PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9933732-5 1999 The effect of exogenous thiamine pyrophosphate (TPP) addition on the blood transketolase (TK) activity (TPP TK effect) served to estimate thiamine deficiency. Thiamine Pyrophosphate 24-46 transketolase Homo sapiens 75-88 9933732-5 1999 The effect of exogenous thiamine pyrophosphate (TPP) addition on the blood transketolase (TK) activity (TPP TK effect) served to estimate thiamine deficiency. Thiamine Pyrophosphate 24-46 transketolase Homo sapiens 90-92 9933732-5 1999 The effect of exogenous thiamine pyrophosphate (TPP) addition on the blood transketolase (TK) activity (TPP TK effect) served to estimate thiamine deficiency. Thiamine Pyrophosphate 48-51 transketolase Homo sapiens 75-88 9933732-5 1999 The effect of exogenous thiamine pyrophosphate (TPP) addition on the blood transketolase (TK) activity (TPP TK effect) served to estimate thiamine deficiency. Thiamine Pyrophosphate 48-51 transketolase Homo sapiens 90-92 9933732-5 1999 The effect of exogenous thiamine pyrophosphate (TPP) addition on the blood transketolase (TK) activity (TPP TK effect) served to estimate thiamine deficiency. Thiamine Pyrophosphate 104-107 transketolase Homo sapiens 75-88 9933732-5 1999 The effect of exogenous thiamine pyrophosphate (TPP) addition on the blood transketolase (TK) activity (TPP TK effect) served to estimate thiamine deficiency. Thiamine Pyrophosphate 104-107 transketolase Homo sapiens 90-92 9933732-9 1999 RESULTS: Of 118 inpatients, 46 (39%) presented with a TPP TK effect of >15%, and 6 with values of >22%, indicating moderate and severe thiamine deficiency, respectively. Thiamine Pyrophosphate 54-57 transketolase Homo sapiens 58-60 9933732-10 1999 Only 6 of 30 outpatients (20%) exhibited a TPP TK effect of >15% and none of them reached values of >18%. Thiamine Pyrophosphate 43-46 transketolase Homo sapiens 47-49 9924800-5 1998 In the homodimer transketolase the two catalytic sites, where dihydroxyethyl groups are transferred from ketose donors to aldose acceptors, are formed at the interface between the two subunits, where the thiazole and pyrimidine rings of thiamin diphosphate are bound. Thiamine Pyrophosphate 237-256 transketolase Homo sapiens 17-30 9924800-1 1998 This review highlights recent research on the properties and functions of the enzyme transketolase, which requires thiamin diphosphate and a divalent metal ion for its activity. Thiamine Pyrophosphate 115-134 transketolase Homo sapiens 85-98 9924800-3 1998 Yeast transketolase is one of several thiamin diphosphate dependent enzymes whose three-dimensional structures have been determined. Thiamine Pyrophosphate 38-57 transketolase Homo sapiens 6-19 9201534-3 1997 Postmortem results revealed low erythrocyte transketolase activity, which was increased by 22% by in vitro addition of thiamine diphosphate (TDP effect). Thiamine Pyrophosphate 119-139 transketolase Homo sapiens 44-57 9655911-3 1998 Thiamin diphosphate (ThDP)-dependent enzymes vary in their substrate tolerance from rather strict substrate specificity (phosphoketolases, glyoxylate carboligase) to more permissive enzymes (transketolase, dihydroxyacetone synthase, pyruvate decarboxylase) and therefore differ in their potential to be used as biocatalysts. Thiamine Pyrophosphate 0-19 transketolase Homo sapiens 191-204 9655911-3 1998 Thiamin diphosphate (ThDP)-dependent enzymes vary in their substrate tolerance from rather strict substrate specificity (phosphoketolases, glyoxylate carboligase) to more permissive enzymes (transketolase, dihydroxyacetone synthase, pyruvate decarboxylase) and therefore differ in their potential to be used as biocatalysts. Thiamine Pyrophosphate 21-25 transketolase Homo sapiens 191-204 9611778-1 1998 Transketolase belongs to the family of thiamin diphosphate dependent enzymes. Thiamine Pyrophosphate 39-58 transketolase Homo sapiens 0-13 9357955-0 1997 Aspartate 155 of human transketolase is essential for thiamine diphosphate-magnesium binding, and cofactor binding is required for dimer formation. Thiamine Pyrophosphate 54-74 transketolase Homo sapiens 23-36 9357955-1 1997 Active human transketolase is a homodimeric enzyme possessing two active sites, each with a non-covalently bound thiamine diphosphate and magnesium. Thiamine Pyrophosphate 113-133 transketolase Homo sapiens 13-26 9194907-4 1997 Transketolase is a homodimeric enzyme containing two molecules of noncovalently bound thiamine pyrophosphate. Thiamine Pyrophosphate 86-108 transketolase Homo sapiens 0-13 9194907-6 1997 Previous findings demonstrated that purified his-transketolase had a Km app for cofactor and a thiamine pyrophosphate-dependent lag period for attaining steady-state kinetics that was similar to transketolase purified from human tissues. Thiamine Pyrophosphate 95-117 transketolase Homo sapiens 49-62 8974135-3 1996 The vitamin B1 level was determined as thiamine pyrophosphate effect on transketolase activity in red blood cell lysates. Thiamine Pyrophosphate 39-61 transketolase Homo sapiens 72-85 8780344-3 1996 Measurements of urinary thiamine and blood transketolase and its activation with thiamine pyrophosphate were made. Thiamine Pyrophosphate 81-103 transketolase Homo sapiens 43-56 7548453-1 1995 The indirect estimation of thiamine levels in human blood by measuring thiamine pyrophosphate effect on erythrocyte transketolase activity is the method of choice in most clinical laboratories. Thiamine Pyrophosphate 71-93 transketolase Homo sapiens 116-129 8683340-5 1996 When exogenous thiamine pyrophosphate was added to the activity assays, differences between transketolase and alpha-KGDH became readily apparent. Thiamine Pyrophosphate 15-37 transketolase Homo sapiens 92-105 8974347-3 1994 We have investigated the interactions of the thiamine-utilizing enzyme transketolase [Tk], derived from human fibroblasts, lymphoblasts, and various brain regions, with its cofactor, thiamine pyrophosphate [TPP], in an attempt to elucidate the molecular basis of selective brain damage in alcoholism-associated thiamine deficiency. Thiamine Pyrophosphate 183-205 transketolase Homo sapiens 71-84 7596328-3 1995 In particular, Tk derived from fibroblasts has been found to have an increased Km app for its cofactor thiamine pyrophosphate [TPP] and/or exist in different isoelectric forms in alcoholic patients with WKS as compared with unaffected individuals. Thiamine Pyrophosphate 103-125 transketolase Homo sapiens 15-17 7596328-3 1995 In particular, Tk derived from fibroblasts has been found to have an increased Km app for its cofactor thiamine pyrophosphate [TPP] and/or exist in different isoelectric forms in alcoholic patients with WKS as compared with unaffected individuals. Thiamine Pyrophosphate 127-130 transketolase Homo sapiens 15-17 7861245-1 1995 We have investigated the hysteretic properties of human transketolase with emphasis on its dependency on thiamine pyrophosphate concentration. Thiamine Pyrophosphate 105-127 transketolase Homo sapiens 56-69 7861245-4 1995 At physiological thiamine pyrophosphate concentrations, the inverse rate constant was in the range of 10 to 20 min for fibroblast-derived transketolase and increased dramatically with only small decreases from these levels of thiamine pyrophosphate. Thiamine Pyrophosphate 17-39 transketolase Homo sapiens 138-151 7861245-4 1995 At physiological thiamine pyrophosphate concentrations, the inverse rate constant was in the range of 10 to 20 min for fibroblast-derived transketolase and increased dramatically with only small decreases from these levels of thiamine pyrophosphate. Thiamine Pyrophosphate 226-248 transketolase Homo sapiens 138-151 8974347-3 1994 We have investigated the interactions of the thiamine-utilizing enzyme transketolase [Tk], derived from human fibroblasts, lymphoblasts, and various brain regions, with its cofactor, thiamine pyrophosphate [TPP], in an attempt to elucidate the molecular basis of selective brain damage in alcoholism-associated thiamine deficiency. Thiamine Pyrophosphate 183-205 transketolase Homo sapiens 86-88 8974347-3 1994 We have investigated the interactions of the thiamine-utilizing enzyme transketolase [Tk], derived from human fibroblasts, lymphoblasts, and various brain regions, with its cofactor, thiamine pyrophosphate [TPP], in an attempt to elucidate the molecular basis of selective brain damage in alcoholism-associated thiamine deficiency. Thiamine Pyrophosphate 207-210 transketolase Homo sapiens 71-84 8974347-3 1994 We have investigated the interactions of the thiamine-utilizing enzyme transketolase [Tk], derived from human fibroblasts, lymphoblasts, and various brain regions, with its cofactor, thiamine pyrophosphate [TPP], in an attempt to elucidate the molecular basis of selective brain damage in alcoholism-associated thiamine deficiency. Thiamine Pyrophosphate 207-210 transketolase Homo sapiens 86-88 8243472-5 1993 The best estimate of the apparent Km, 1.59 +/- 0.23 microM, for the binding of Mg(2+)-thiamin diphosphate to transketolase was obtained in the presence of a high non-inhibitory concentration of magnesium and varied concentrations of thiamin diphosphate. Thiamine Pyrophosphate 86-105 transketolase Homo sapiens 109-122 8069629-0 1993 A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Thiamine Pyrophosphate 2-21 transketolase Homo sapiens 87-100 2210959-0 1990 The relationship between the thiamin pyrophosphate effect and the saturation status of the transketolase with its coenzyme in human erythrocytes. Thiamine Pyrophosphate 29-50 transketolase Homo sapiens 91-104 1297775-2 1992 The activities of 3 TPP-dependent enzymes are reduced in DAT brain: transketolase (TK), the pyruvate dehydrogenase complex (PDHC), and the alpha-ketoglutarate dehydrogenase complex (KGDHC). Thiamine Pyrophosphate 20-23 transketolase Homo sapiens 83-85 1807869-1 1991 In 60 thiamine deficient patients, the mean erythrocyte transketolase activity after activation by thiamine diphosphate cofactor in vitro, representing the apparent sum of holoenzyme and apoenzyme activities, was 0.609 (SD 0.166) U/g Hb before thiamine therapy and rose to 0.772 (SD 0.152) U/g Hb immediately after the administration of thiamine to the patients. Thiamine Pyrophosphate 99-119 transketolase Homo sapiens 56-69 1807869-2 1991 The difference between these values, 0.163 (SD 0.130) U/g, is the mean activity of transketolase protein which can be activated by thiamine in vivo but not by thiamine diphosphate in vitro. Thiamine Pyrophosphate 159-179 transketolase Homo sapiens 83-96 8279670-2 1993 Results of this study demonstrate significant reductions of TPP-dependent enzymes [pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase (alpha KGDH), and transketolase] in autopsied cerebellar vermis samples from alcoholic patients with the clinical and neuropathologically confirmed diagnosis of Wernicke-Korsakoff Syndrome (WKS). Thiamine Pyrophosphate 60-63 transketolase Homo sapiens 167-180 8419340-1 1993 Variants of the enzyme transketolase which possess reduced affinity for its cofactor thiamine pyrophosphate (high apparent Km) have been described in chronic alcoholic patients with Wernicke-Korsakoff syndrome. Thiamine Pyrophosphate 85-107 transketolase Homo sapiens 23-36 1297775-2 1992 The activities of 3 TPP-dependent enzymes are reduced in DAT brain: transketolase (TK), the pyruvate dehydrogenase complex (PDHC), and the alpha-ketoglutarate dehydrogenase complex (KGDHC). Thiamine Pyrophosphate 20-23 transketolase Homo sapiens 68-81 2307803-3 1990 Each of three individuals responded clinically to the administration of thiamin tetrahydrofurfuryl disulfide (TTFD), and erythrocyte transketolase (TKA) became fully saturated with thiamin pyrophosphate (TPP). Thiamine Pyrophosphate 181-202 transketolase Homo sapiens 148-151 2307803-3 1990 Each of three individuals responded clinically to the administration of thiamin tetrahydrofurfuryl disulfide (TTFD), and erythrocyte transketolase (TKA) became fully saturated with thiamin pyrophosphate (TPP). Thiamine Pyrophosphate 204-207 transketolase Homo sapiens 148-151 2136519-9 1990 In assaying for red-cell transketolase levels, this subgroup showed higher thiamin pyrophosphate effects than did the whole sample. Thiamine Pyrophosphate 75-96 transketolase Homo sapiens 25-38 2210959-2 1990 But there has not been any report concerning whether or not the thiamin pyrophosphate effect really reflects the saturation status of transketolase with thiamin pyrophosphate. Thiamine Pyrophosphate 153-174 transketolase Homo sapiens 134-147 2210959-3 1990 In this report we studied the relationship between the thiamin pyrophosphate effect and the saturation status of transketolase. Thiamine Pyrophosphate 55-76 transketolase Homo sapiens 113-126 2210959-5 1990 The molar ratio of thiamin pyrophosphate to transketolase was in inverse proportion to the thiamin pyrophosphate effect. Thiamine Pyrophosphate 19-40 transketolase Homo sapiens 44-57 2210959-5 1990 The molar ratio of thiamin pyrophosphate to transketolase was in inverse proportion to the thiamin pyrophosphate effect. Thiamine Pyrophosphate 91-112 transketolase Homo sapiens 44-57 2210959-8 1990 These results indicate that the thiamin pyrophosphate effect really reflects the saturation status of transketolase with coenzyme. Thiamine Pyrophosphate 32-53 transketolase Homo sapiens 102-115 2675860-3 1989 TPP is a cofactor for the pyruvate dehydrogenase complex (PDHC), alpha-ketoglutarate dehydrogenase (alpha KGDH) and transketolase (TK), three enzymes involved in cerebral glucose and energy metabolism. Thiamine Pyrophosphate 0-3 transketolase Homo sapiens 116-129 34161071-1 2021 A computational model for human transketolase was proposed, showing that thiamine diphosphate activation was based on His110 in place of His481 reported in yeast transketolase. Thiamine Pyrophosphate 73-93 transketolase Homo sapiens 32-45 34161071-1 2021 A computational model for human transketolase was proposed, showing that thiamine diphosphate activation was based on His110 in place of His481 reported in yeast transketolase. Thiamine Pyrophosphate 73-93 transketolase Homo sapiens 162-175 2799573-4 1989 The transketolase response to thiamine pyrophosphate (TPP effect) suggested thiamine deficiency in 32.4%, of whom 13.2% were classified as severely deficient. Thiamine Pyrophosphate 30-52 transketolase Homo sapiens 4-17 2675860-3 1989 TPP is a cofactor for the pyruvate dehydrogenase complex (PDHC), alpha-ketoglutarate dehydrogenase (alpha KGDH) and transketolase (TK), three enzymes involved in cerebral glucose and energy metabolism. Thiamine Pyrophosphate 0-3 transketolase Homo sapiens 131-133 3558815-2 1987 This study was undertaken to delineate whether transketolase abnormality (i.e., high Michaelis Menton constant (Km) for thiamine pyrophosphate), previously reported in patients with Wernicke-Korsakoff syndrome is prevalent among familial chronic alcoholic men and their sons without prior history of alcohol abuse but who are at high risk for alcoholism. Thiamine Pyrophosphate 120-142 transketolase Homo sapiens 47-60 3129964-3 1988 Transketolase concentration correlated positively with the enzyme activity both with and without in vitro addition of thiamin pyrophosphate. Thiamine Pyrophosphate 118-139 transketolase Homo sapiens 0-13 3248678-0 1988 Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes. Thiamine Pyrophosphate 25-47 transketolase Homo sapiens 94-107 3602224-1 1987 Erythrocyte transketolase activation by thiamin diphosphate has been studied in elderly patients with moderate or severe chronic dementia, acute alcoholic admissions and chronic alcoholics with evidence of brain damage, mostly of the Wernicke-Korsakoff type. Thiamine Pyrophosphate 40-59 transketolase Homo sapiens 12-25 3602224-2 1987 Significantly more patients in each group than controls showed abnormal activation of transketolase, not only by 0.3 mM thiamin diphosphate (TDP) but also in further activation by increase to 3 mM. Thiamine Pyrophosphate 120-139 transketolase Homo sapiens 86-99 3426764-1 1987 Erythrocyte transketolase activation by thiamin diphosphate has been studied in alcoholic patients on admission and after treatment, which included vitamin therapy. Thiamine Pyrophosphate 40-59 transketolase Homo sapiens 12-25 3426764-2 1987 The high proportion of the patients who showed an abnormal activation of transketolase, not only by 0.3 mM thiamin diphosphate but also further activation by increasing the thiamin diphosphate to 3 mM, was reduced considerably after treatment. Thiamine Pyrophosphate 107-126 transketolase Homo sapiens 73-86 3426764-2 1987 The high proportion of the patients who showed an abnormal activation of transketolase, not only by 0.3 mM thiamin diphosphate but also further activation by increasing the thiamin diphosphate to 3 mM, was reduced considerably after treatment. Thiamine Pyrophosphate 173-192 transketolase Homo sapiens 73-86 3762968-1 1986 We studied a thiamine-dependent enzyme, transketolase, from fibroblasts of a diabetic patient who developed Wernicke"s encephalopathy when treated with tolazamide, in order to delineate if this patient also had transketolase abnormality [high Km for thiamine pyrophosphate (TPP)], as previously reported in postalcoholic Wernicke-Korsakoff syndrome. Thiamine Pyrophosphate 250-272 transketolase Homo sapiens 40-53 3762968-1 1986 We studied a thiamine-dependent enzyme, transketolase, from fibroblasts of a diabetic patient who developed Wernicke"s encephalopathy when treated with tolazamide, in order to delineate if this patient also had transketolase abnormality [high Km for thiamine pyrophosphate (TPP)], as previously reported in postalcoholic Wernicke-Korsakoff syndrome. Thiamine Pyrophosphate 274-277 transketolase Homo sapiens 40-53 3762968-3 1986 We found that the above-mentioned patient and one of the diabetic kindreds with no history of Wernicke"s encephalopathy had abnormal transketolase as determined by its Km for TPP. Thiamine Pyrophosphate 175-178 transketolase Homo sapiens 133-146 3558815-3 1987 Our data suggest that an inborn error (i.e., high Km of transketolase for thiamine pyrophosphate) predisposing to thiamine deficiency diseases similar to those reported in Wernicke-Korsakoff syndrome may occur in the general population. Thiamine Pyrophosphate 74-96 transketolase Homo sapiens 56-69 6497956-4 1984 Not only do the apoenzymes isolated from each of the two fractions differ in the way in which they recombine with thiamine pyrophosphate but kinetic analysis of the results shows that each fraction contains at least two variants of transketolase differing in their affinity for thiamine pyrophosphate. Thiamine Pyrophosphate 114-136 transketolase Homo sapiens 232-245 4052157-3 1985 It is concluded that the failure to detect an increase in activation in the commonly used clinical test of red cell transketolase activation by raising the thiamine diphosphate concentration above about 0.3 mmol/l is likely to be due to masking of the effect of activation of the low affinity variant in haemolysates from normal red blood cells by the inhibitory effect of excess thiamine diphosphate upon the activity of the high affinity form of the enzyme with which it is mixed. Thiamine Pyrophosphate 156-176 transketolase Homo sapiens 116-129 6434322-6 1984 This association suggests that a variant transketolase and thiamin deficiency together contribute to the pathogenesis of the brain damage of the Wernicke-Korsakoff syndrome by some mechanism independent of apparent Km values for thiamin diphosphate. Thiamine Pyrophosphate 229-248 transketolase Homo sapiens 41-54 6191889-5 1983 The addition of thiamin diphosphate to the staining mixture darkened some but not all bands of transketolase activity. Thiamine Pyrophosphate 16-35 transketolase Homo sapiens 95-108 6191889-7 1983 This heterogeneity might need recognition when thiamin nutritional sufficiency is assessed by the "thiamin diphosphate effect" on erythrocyte transketolase. Thiamine Pyrophosphate 99-118 transketolase Homo sapiens 142-155 6649520-1 1983 In blood of patients with cancer of stomach and mammary gland total thiamin content was measured by means of fluorimetric procedure, thiamindiphosphate (TDP)--by an enzymatic method, activity of transketolase was estimated in presence or in absence of TDP. Thiamine Pyrophosphate 133-151 transketolase Homo sapiens 195-208 6649520-2 1983 Concentration of total thiamin in blood of healthy persons was 7.65 +/- 0.40 micrograms/100 ml; thiamindiphosphate--5.06 micrograms/100 ml activity of transketolase was 11.59 +/- 0.23 mmol/l. Thiamine Pyrophosphate 96-114 transketolase Homo sapiens 151-164 6497956-4 1984 Not only do the apoenzymes isolated from each of the two fractions differ in the way in which they recombine with thiamine pyrophosphate but kinetic analysis of the results shows that each fraction contains at least two variants of transketolase differing in their affinity for thiamine pyrophosphate. Thiamine Pyrophosphate 278-300 transketolase Homo sapiens 232-245 6139882-14 1983 Finally focus is set on the recent suggestion that the syndrome may in some cases result from an inborn enzymatic abnormality comprising low binding of thiamine pyrophosphate to transketolase. Thiamine Pyrophosphate 152-174 transketolase Homo sapiens 178-191 6115895-6 1981 Red blood cells from this group of kittens also showed a transitory incomplete saturation of transketolase with thiamin pyrophosphate. Thiamine Pyrophosphate 112-133 transketolase Homo sapiens 93-106 7113098-1 1982 A modified method is described for determination of transketolase (TK) activity in the blood and the degree of its stimulation under the effect of exogenous thiamine diphosphate (TDP-effect). Thiamine Pyrophosphate 157-177 transketolase Homo sapiens 52-65 7113098-1 1982 A modified method is described for determination of transketolase (TK) activity in the blood and the degree of its stimulation under the effect of exogenous thiamine diphosphate (TDP-effect). Thiamine Pyrophosphate 157-177 transketolase Homo sapiens 67-69 7223515-1 1981 The thiamine contents, transketolase activity and "thiamine diphosphate effect" (TDP effect) of the transketolase activity were measured in the blood of alcoholic patients during withdrawal, before and after thiamine administration (50 mg) for 10 days. Thiamine Pyrophosphate 51-71 transketolase Homo sapiens 100-113 7270482-1 1981 A semiautomated method is described which uses the Abbott ABA-100 bichromatic analyzer to measure the stimulation of erythrocyte transketolase by thiamin pyrophosphate (the thiamin pyrophosphate effect). Thiamine Pyrophosphate 146-167 transketolase Homo sapiens 129-142 7270482-1 1981 A semiautomated method is described which uses the Abbott ABA-100 bichromatic analyzer to measure the stimulation of erythrocyte transketolase by thiamin pyrophosphate (the thiamin pyrophosphate effect). Thiamine Pyrophosphate 173-194 transketolase Homo sapiens 129-142 6256098-3 1980 The values of the transketolase activity of the two groups were statistically correlated with the levels of the thiamine pyrophosphate effect and the vitamin B1 content of the blood. Thiamine Pyrophosphate 112-134 transketolase Homo sapiens 18-31 7405142-7 1980 The results obtained indicate high transketolase saturation with thiamine diphosphate with low thiamine concentration in blood. Thiamine Pyrophosphate 65-85 transketolase Homo sapiens 35-48 7438971-5 1980 In the second case, red cell transketolase indicated thiamine pyrophosphate deficiency. Thiamine Pyrophosphate 53-75 transketolase Homo sapiens 29-42 228770-3 1979 The anticoenzymic effect of hydroxythiamine pyrophosphate with respect to transketolase is not observed in vivo at maximal concentration of the anticoenzyme in tissues due to the absence of competitive interactions with thiamine pyrophosphate. Thiamine Pyrophosphate 35-57 transketolase Homo sapiens 74-87 453718-2 1979 This intermediate product of glucose metabolism is the result of transketolase activity for which thiamine pyrophosphate is one of the co-factors. Thiamine Pyrophosphate 98-120 transketolase Homo sapiens 65-78 4564138-0 1972 [Interaction of thiamine pyrophosphate and transketolase]. Thiamine Pyrophosphate 16-38 transketolase Homo sapiens 43-56 1253408-1 1976 We describe optimized, ultraviolet spectrophotometric procedures for determination of erythrocyte transketolase, glutathione reductase, and aspartate aminotransferase activity, and their activation by their respective coenzymes--thiamine pyrophosphate, flavin-adenine dinucleotide, and pyridoxal-5-phosphate--as tests for vitamin B1, B2, and B6 deficiency. Thiamine Pyrophosphate 229-251 transketolase Homo sapiens 98-111 1262137-4 1976 The thiamine status was measured by determining the thiamine pyrophosphate stimulating effect of transketolase enzyme activity in whole blood. Thiamine Pyrophosphate 52-74 transketolase Homo sapiens 97-110 627916-0 1978 The determination of thiamin pyrophosphate in blood and other tissues, and its correlation with erythrocyte transketolase activity. Thiamine Pyrophosphate 21-42 transketolase Homo sapiens 108-121 927453-2 1977 Transketolase in fibroblasts from the patients with the syndrome bound thiamine pyrophosphate less avidly than control lines. Thiamine Pyrophosphate 71-93 transketolase Homo sapiens 0-13 927453-3 1977 The apparent Km for thiamine pyrophosphate was 195 +/- 31 micron for transketolase in extracts of the patients" cells as compared to 16 +/- 2 micron in six control lines (means +/- S.E.M. Thiamine Pyrophosphate 20-42 transketolase Homo sapiens 69-82 1093550-0 1975 The binding of thiamine pyrophosphate with transketolase in equilibrium conditions. Thiamine Pyrophosphate 15-37 transketolase Homo sapiens 43-56 23440198-1 2013 A transketolase reaction was catalyzed by cyanide ion under prebiotic conditions instead of its modern catalyst, thiamine pyrophosphate (TPP). Thiamine Pyrophosphate 113-135 transketolase Homo sapiens 2-15 5096513-5 1971 The specific effect on transketolase by uremic material was established by showing suppressed formation of S7P from R5P also in the presence of excess cofactor thiamine pyrophosphate and of the other substrate xylulose-5-phosphate. Thiamine Pyrophosphate 160-182 transketolase Homo sapiens 23-36 33354793-4 2021 Thiamine diphosphate is a cofactor for transketolase, including erythrocyte transketolase (ETK). Thiamine Pyrophosphate 0-20 transketolase Homo sapiens 39-52 28950391-3 2018 We hypothesized that protective PPP action in diabetes and eventually even more severely in concomitant DKD might be compromised by limited intracellular availability of an active TKT cofactor thiamine diphosphate (TDP). Thiamine Pyrophosphate 193-213 transketolase Homo sapiens 180-183 33217405-2 2021 In a recent paper, we showed the difference between the first stage of the one-substrate and the two-substrate transketolase reactions - the possibility of transfer of glycolaldehyde formed as a result of cleavage of the donor substrate from the thiazole ring of thiamine diphosphate to its aminopyrimidine ring through the tricycle formation stage, which is necessary for binding and splitting the second molecule of donor substrate [O.N. Thiamine Pyrophosphate 263-283 transketolase Homo sapiens 111-124 33217405-6 2021 Therefore, a significant decrease in the reaction rate of the one-substrate transketolase reaction compared to the two-substrate reaction is due to the stage of transferring the first glycolaldehyde molecule from the thiazole ring to the aminopyrimidine ring of thiamine diphosphate. Thiamine Pyrophosphate 262-282 transketolase Homo sapiens 76-89 32139871-1 2020 We recently characterised a low-activity form of E. coli transketolase, TKlow, which also binds the cofactor thiamine pyrophosphate (TPP) with an affinity up to two-orders of magnitude lower than the previously known high TPP-affinity and high-activity form, TKhigh, in the presence of Mg2+. Thiamine Pyrophosphate 109-131 transketolase Homo sapiens 57-70 32139871-1 2020 We recently characterised a low-activity form of E. coli transketolase, TKlow, which also binds the cofactor thiamine pyrophosphate (TPP) with an affinity up to two-orders of magnitude lower than the previously known high TPP-affinity and high-activity form, TKhigh, in the presence of Mg2+. Thiamine Pyrophosphate 133-136 transketolase Homo sapiens 57-70 32139871-1 2020 We recently characterised a low-activity form of E. coli transketolase, TKlow, which also binds the cofactor thiamine pyrophosphate (TPP) with an affinity up to two-orders of magnitude lower than the previously known high TPP-affinity and high-activity form, TKhigh, in the presence of Mg2+. Thiamine Pyrophosphate 222-225 transketolase Homo sapiens 57-70 32139871-4 2020 Transketolase HPA affinity again revealed the two distinct forms of transketolase at a TKhigh:TKlow ratio that matched those observed previously via TPP binding to each variant. Thiamine Pyrophosphate 149-152 transketolase Homo sapiens 68-81 31695144-1 2019 Transketolase (TK) cofactor binding has been studied extensively over many years, yet certain mysteries remain, such as a lack of consensus on the cooperativity of thiamine pyrophosphate (TPP) binding into the two active sites, in the presence and absence of the divalent cation, Mg2+. Thiamine Pyrophosphate 164-186 transketolase Homo sapiens 0-13 31695144-1 2019 Transketolase (TK) cofactor binding has been studied extensively over many years, yet certain mysteries remain, such as a lack of consensus on the cooperativity of thiamine pyrophosphate (TPP) binding into the two active sites, in the presence and absence of the divalent cation, Mg2+. Thiamine Pyrophosphate 188-191 transketolase Homo sapiens 0-13 31415630-3 2019 Transketolase (TKT) is a thiamine pyrophosphate (vitamin B1)-dependent enzyme that links the pentose phosphate pathway with the glycolytic pathway by feeding excess sugar phosphates into the main carbohydrate metabolic pathways to generate biosynthetic reducing capacity in the form of NADPH as a substrate for ROS generation. Thiamine Pyrophosphate 25-47 transketolase Homo sapiens 0-13 31415630-3 2019 Transketolase (TKT) is a thiamine pyrophosphate (vitamin B1)-dependent enzyme that links the pentose phosphate pathway with the glycolytic pathway by feeding excess sugar phosphates into the main carbohydrate metabolic pathways to generate biosynthetic reducing capacity in the form of NADPH as a substrate for ROS generation. Thiamine Pyrophosphate 25-47 transketolase Homo sapiens 15-18 26998737-1 2016 We propose the first computational model for transketolase (TK), a thiamine diphosphate (ThDP)-dependent enzyme, using a quantum mechanical/molecular mechanical method on the basis of crystallographic TK structures from yeast and Escherichia coli, together with experimental kinetic data reported in the literature with wild-type and mutant TK. Thiamine Pyrophosphate 67-87 transketolase Homo sapiens 45-58 26998737-1 2016 We propose the first computational model for transketolase (TK), a thiamine diphosphate (ThDP)-dependent enzyme, using a quantum mechanical/molecular mechanical method on the basis of crystallographic TK structures from yeast and Escherichia coli, together with experimental kinetic data reported in the literature with wild-type and mutant TK. Thiamine Pyrophosphate 89-93 transketolase Homo sapiens 45-58 25267444-3 2014 In contrast, transketolase and phosphoketolase make use of the bioorganic cofactor thiamin diphosphate to cleave the preceding C2-C3 bond of ketose phosphates. Thiamine Pyrophosphate 83-102 transketolase Homo sapiens 13-26 23440198-1 2013 A transketolase reaction was catalyzed by cyanide ion under prebiotic conditions instead of its modern catalyst, thiamine pyrophosphate (TPP). Thiamine Pyrophosphate 137-140 transketolase Homo sapiens 2-15 20673211-3 2010 The amount of active transketolase in the isolated protein preparation was correlated with the content of thiamine diphosphate (ThDP) determined in the same preparation. Thiamine Pyrophosphate 106-126 transketolase Homo sapiens 21-34 24114639-1 2013 INTRODUCTION: The activity of erythrocyte transketolase induced by thiamine pyrophosphate and normalized to age of the patient is a marker of thiamine metabolism disturbances with pathological consequences in the central and peripheral nervous system. Thiamine Pyrophosphate 67-89 transketolase Homo sapiens 42-55 24114639-14 2013 Abnormalities in transketolase activity, when expressed in three modalities: basal activity, normalized transketolase activity ratio and the activity after the stimulation with thiamine pyrophosphate may be differentiated as thiamine-dependent or resulting from posttranslational modification. Thiamine Pyrophosphate 177-199 transketolase Homo sapiens 17-30 21288652-3 2011 TPP is a relevant cofactor for transketolase (TK), alpha-ketoglutarate dehydrogenase (alphaKDH), and pyruvate dehydrogenase (PDH), all these enzymes are fundamental for glucose metabolism. Thiamine Pyrophosphate 0-3 transketolase Homo sapiens 31-44 21288652-3 2011 TPP is a relevant cofactor for transketolase (TK), alpha-ketoglutarate dehydrogenase (alphaKDH), and pyruvate dehydrogenase (PDH), all these enzymes are fundamental for glucose metabolism. Thiamine Pyrophosphate 0-3 transketolase Homo sapiens 46-48 20667822-1 2010 The crystal structure of human transketolase (TKT), a thiamine diphosphate (ThDP) and Ca(2+)-dependent enzyme that catalyzes the interketol transfer between ketoses and aldoses as part of the pentose phosphate pathway, has been determined to 1.75 A resolution. Thiamine Pyrophosphate 54-74 transketolase Homo sapiens 31-44 20667822-1 2010 The crystal structure of human transketolase (TKT), a thiamine diphosphate (ThDP) and Ca(2+)-dependent enzyme that catalyzes the interketol transfer between ketoses and aldoses as part of the pentose phosphate pathway, has been determined to 1.75 A resolution. Thiamine Pyrophosphate 54-74 transketolase Homo sapiens 46-49 20667822-1 2010 The crystal structure of human transketolase (TKT), a thiamine diphosphate (ThDP) and Ca(2+)-dependent enzyme that catalyzes the interketol transfer between ketoses and aldoses as part of the pentose phosphate pathway, has been determined to 1.75 A resolution. Thiamine Pyrophosphate 76-80 transketolase Homo sapiens 31-44 20667822-1 2010 The crystal structure of human transketolase (TKT), a thiamine diphosphate (ThDP) and Ca(2+)-dependent enzyme that catalyzes the interketol transfer between ketoses and aldoses as part of the pentose phosphate pathway, has been determined to 1.75 A resolution. Thiamine Pyrophosphate 76-80 transketolase Homo sapiens 46-49 20667822-5 2010 The cofactor and substrate binding sites of human TKT bear high resemblance to those of other TKTs but also feature unique properties, including two lysines and a serine that interact with the beta-phosphate of ThDP. Thiamine Pyrophosphate 211-215 transketolase Homo sapiens 50-53 20673211-3 2010 The amount of active transketolase in the isolated protein preparation was correlated with the content of thiamine diphosphate (ThDP) determined in the same preparation. Thiamine Pyrophosphate 128-132 transketolase Homo sapiens 21-34 20673211-4 2010 Induced optical activity, facilitating studies of ThDP binding by the apoenzyme and measurement of the transketolase reaction at each stage, was detected by circular dichroism spectroscopy. Thiamine Pyrophosphate 50-54 transketolase Homo sapiens 103-116 20188835-5 2010 Benfotiamine administration increases the levels of intracellular thiamine diphosphate, a cofactor necessary for the activation transketolase, resulting in the reduction of tissue level of AGEs. Thiamine Pyrophosphate 66-86 transketolase Homo sapiens 128-141 19290028-1 2009 Transketolase (TK), a thiamine diphosphate (ThDP)-dependent enzyme, catalyzes several key reactions of non-oxidative branch of pentose phosphate pathway. Thiamine Pyrophosphate 22-42 transketolase Homo sapiens 0-13 18490188-2 2009 In its active form, thiamin pyrophosphate (TPP), it is a co-enzyme for several enzymes, including transketolase. Thiamine Pyrophosphate 20-41 transketolase Homo sapiens 98-111 18490188-2 2009 In its active form, thiamin pyrophosphate (TPP), it is a co-enzyme for several enzymes, including transketolase. Thiamine Pyrophosphate 43-46 transketolase Homo sapiens 98-111 19290028-1 2009 Transketolase (TK), a thiamine diphosphate (ThDP)-dependent enzyme, catalyzes several key reactions of non-oxidative branch of pentose phosphate pathway. Thiamine Pyrophosphate 22-42 transketolase Homo sapiens 15-17 19290028-1 2009 Transketolase (TK), a thiamine diphosphate (ThDP)-dependent enzyme, catalyzes several key reactions of non-oxidative branch of pentose phosphate pathway. Thiamine Pyrophosphate 44-48 transketolase Homo sapiens 0-13 19290028-1 2009 Transketolase (TK), a thiamine diphosphate (ThDP)-dependent enzyme, catalyzes several key reactions of non-oxidative branch of pentose phosphate pathway. Thiamine Pyrophosphate 44-48 transketolase Homo sapiens 15-17 19290028-3 2009 Both ThDP and bivalent cations are strictly needed for TK activation, just like that for all ThDP-dependent enzymes. Thiamine Pyrophosphate 5-9 transketolase Homo sapiens 55-57 19290028-3 2009 Both ThDP and bivalent cations are strictly needed for TK activation, just like that for all ThDP-dependent enzymes. Thiamine Pyrophosphate 93-97 transketolase Homo sapiens 55-57 17914867-1 2007 Transketolase is a prominent thiamin diphosphate-dependent enzyme in sugar metabolism that catalyzes the reversible transfer of a 2-carbon dihydroxyethyl fragment between a donor ketose and an acceptor aldose. Thiamine Pyrophosphate 29-48 transketolase Homo sapiens 0-13 19364324-1 2009 In this work, we investigated the rate of formation of the central intermediate of the transketolase reaction with thiamine diphosphate (ThDP) or 4"-methylamino-ThDP as cofactors and its stability using stopped-flow spectroscopy and circular dichroism (CD) spectroscopy. Thiamine Pyrophosphate 115-135 transketolase Homo sapiens 87-100 19364324-1 2009 In this work, we investigated the rate of formation of the central intermediate of the transketolase reaction with thiamine diphosphate (ThDP) or 4"-methylamino-ThDP as cofactors and its stability using stopped-flow spectroscopy and circular dichroism (CD) spectroscopy. Thiamine Pyrophosphate 137-141 transketolase Homo sapiens 87-100 19364324-6 2009 These data suggest that transketolase in the complex with the NH2-methylated ThDP exhibits dihydroxyethyl-4"-methylamino-ThDP-synthase activity. Thiamine Pyrophosphate 77-81 transketolase Homo sapiens 24-37 19111488-5 2009 In addition, an interaction analysis of its cofactor (thiamine pyrophosphate) and a binding site description were carried out, suggesting the substrate channel already identified in yeast Transketolase. Thiamine Pyrophosphate 54-76 transketolase Homo sapiens 188-201 15511224-5 2004 The influence of the donor substrate on the coenzyme-apotransketolase interaction was predicted as a result of formation of the transketolase reaction intermediate 2-(alpha,beta-dihydroxyethyl)-thiamin diphosphate, which exhibited a higher affinity to the enzyme than thiamin diphosphate. Thiamine Pyrophosphate 194-213 transketolase Homo sapiens 56-69 17454302-6 2007 2004, 271, 4189 - 4194) we reported that the affinity of ThDP for TK considerably increases in the presence of the donor substrate, which may be a mechanism whereby the activity of the enzyme is regulated under the conditions of the coenzyme deficiency. Thiamine Pyrophosphate 57-61 transketolase Homo sapiens 66-68 17309441-0 2007 Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase. Thiamine Pyrophosphate 54-74 transketolase Homo sapiens 86-99 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 41-61 transketolase Homo sapiens 74-87 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 41-61 transketolase Homo sapiens 89-91 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 41-61 transketolase Homo sapiens 111-113 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 41-61 transketolase Homo sapiens 111-113 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 41-61 transketolase Homo sapiens 111-113 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 63-67 transketolase Homo sapiens 74-87 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 63-67 transketolase Homo sapiens 89-91 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 63-67 transketolase Homo sapiens 111-113 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 63-67 transketolase Homo sapiens 111-113 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 63-67 transketolase Homo sapiens 111-113 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 116-120 transketolase Homo sapiens 74-87 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 116-120 transketolase Homo sapiens 89-91 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 116-120 transketolase Homo sapiens 74-87 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 116-120 transketolase Homo sapiens 89-91 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 116-120 transketolase Homo sapiens 74-87 17309441-1 2007 The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP <--> TK...ThDP <--> TK*-ThDP. Thiamine Pyrophosphate 116-120 transketolase Homo sapiens 89-91 17309441-2 2007 The scheme involves the formation of inactive intermediate complex TK...ThDP followed by its transformation into catalytically active holoenzyme, TK*-ThDP. Thiamine Pyrophosphate 72-76 transketolase Homo sapiens 67-69 17309441-2 2007 The scheme involves the formation of inactive intermediate complex TK...ThDP followed by its transformation into catalytically active holoenzyme, TK*-ThDP. Thiamine Pyrophosphate 72-76 transketolase Homo sapiens 146-148 17309441-2 2007 The scheme involves the formation of inactive intermediate complex TK...ThDP followed by its transformation into catalytically active holoenzyme, TK*-ThDP. Thiamine Pyrophosphate 150-154 transketolase Homo sapiens 67-69 17309441-2 2007 The scheme involves the formation of inactive intermediate complex TK...ThDP followed by its transformation into catalytically active holoenzyme, TK*-ThDP. Thiamine Pyrophosphate 150-154 transketolase Homo sapiens 146-148 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 19-39 transketolase Homo sapiens 52-65 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 19-39 transketolase Homo sapiens 67-69 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 19-39 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 19-39 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 41-45 transketolase Homo sapiens 52-65 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 41-45 transketolase Homo sapiens 67-69 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 41-45 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 41-45 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 52-65 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 67-69 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 52-65 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 67-69 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 179-181 17454302-1 2007 The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP). Thiamine Pyrophosphate 184-188 transketolase Homo sapiens 179-181 15511224-6 2004 The enhancement of thiamin diphosphate"s affinity to apotransketolase in the presence of donor substrate is probably one of the mechanisms underlying the substrate-affected transketolase regulation at low coenzyme concentrations. Thiamine Pyrophosphate 19-38 transketolase Homo sapiens 56-69 11736629-1 2001 Transketolase is the simplest representative of the thiamine diphosphate-dependent enzymes. Thiamine Pyrophosphate 52-72 transketolase Homo sapiens 0-13 12693972-8 2003 According to our hypothesis, the induced absorption band is that of the imino form of ThDP resulting from three contributing features of the ThDP binding site of transketolase: the relative hydrophobicity of this site, hydrogen bonding of the N1;-atom of the ThDP aminopyrimidine ring to Glu418, and base stacking interactions between the aminopyrimidine ring of ThDP and Phe445. Thiamine Pyrophosphate 86-90 transketolase Homo sapiens 162-175 12693972-8 2003 According to our hypothesis, the induced absorption band is that of the imino form of ThDP resulting from three contributing features of the ThDP binding site of transketolase: the relative hydrophobicity of this site, hydrogen bonding of the N1;-atom of the ThDP aminopyrimidine ring to Glu418, and base stacking interactions between the aminopyrimidine ring of ThDP and Phe445. Thiamine Pyrophosphate 141-145 transketolase Homo sapiens 162-175 12693972-8 2003 According to our hypothesis, the induced absorption band is that of the imino form of ThDP resulting from three contributing features of the ThDP binding site of transketolase: the relative hydrophobicity of this site, hydrogen bonding of the N1;-atom of the ThDP aminopyrimidine ring to Glu418, and base stacking interactions between the aminopyrimidine ring of ThDP and Phe445. Thiamine Pyrophosphate 141-145 transketolase Homo sapiens 162-175 12693972-8 2003 According to our hypothesis, the induced absorption band is that of the imino form of ThDP resulting from three contributing features of the ThDP binding site of transketolase: the relative hydrophobicity of this site, hydrogen bonding of the N1;-atom of the ThDP aminopyrimidine ring to Glu418, and base stacking interactions between the aminopyrimidine ring of ThDP and Phe445. Thiamine Pyrophosphate 141-145 transketolase Homo sapiens 162-175 10622704-2 1999 p-Hydroxyphenylpyruvate proved to be a reversible and competitive inhibitor of transketolase with respect to substrate; it was also able to displace thiamine diphosphate from holotransketolase. Thiamine Pyrophosphate 149-169 transketolase Homo sapiens 79-92 10466187-2 1999 It has been suggested that the Wernicke-Korsakoff syndrome is associated with a genetic variant of transketolase which requires a higher than normal concentration of thiamin diphosphate for activity. Thiamine Pyrophosphate 166-185 transketolase Homo sapiens 99-112