PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24913741-5 2014 Subsequently, NADH is used in the conversion of resazurin to fluorescent resorufin by DI. NAD 14-18 dihydrolipoamide dehydrogenase Homo sapiens 86-88 20507824-7 2010 Then the oxidized state of DI was regenerated into its reduced native state by its natural substrate, nicotinamide adenine dinucleotide (NADH). NAD 102-135 dihydrolipoamide dehydrogenase Homo sapiens 27-29 23832307-8 2013 Here we present a diaphorase/lactate dehydrogenase NAD cycling assay optimized for hESCs, together with a mechanism-based, nonlinear regression models for the determination of NAD(+), NADH, and total NAD. NAD 51-54 dihydrolipoamide dehydrogenase Homo sapiens 18-28 22497727-0 2012 In situ regeneration of NADH via lipoamide dehydrogenase-catalyzed electron transfer reaction evidenced by spectroelectrochemistry. NAD 24-28 dihydrolipoamide dehydrogenase Homo sapiens 33-56 22497727-2 2012 We report on characterizations of in situ regeneration of NADH via lipoamide dehydrogenase (LD)-catalyzed electron transfer reaction to regenerate NADH using UV-vis spectroelectrochemistry. NAD 58-62 dihydrolipoamide dehydrogenase Homo sapiens 67-90 22497727-2 2012 We report on characterizations of in situ regeneration of NADH via lipoamide dehydrogenase (LD)-catalyzed electron transfer reaction to regenerate NADH using UV-vis spectroelectrochemistry. NAD 147-151 dihydrolipoamide dehydrogenase Homo sapiens 67-90 21930696-4 2011 We analyzed human DLD mutations linked to strikingly different clinical phenotypes, including E340K, D444V, R447G, and R460G in the dimer interface domain that are responsible for severe multisystem disorders of infancy and G194C in the NAD(+)-binding domain that is typically associated with milder presentations. NAD 237-243 dihydrolipoamide dehydrogenase Homo sapiens 18-21 23734016-5 2013 The generation of NAD can be coupled to a cycling assay using the enzymes alcohol dehydrogenase and diaphorase. NAD 18-21 dihydrolipoamide dehydrogenase Homo sapiens 100-110 23339632-2 2013 Results showed that diaphorase (DP) and lactate dehydrogenases (LDH) had distinct binding selectivity and preference over reduced and oxidized states of coenzyme NAD(H). NAD 162-168 dihydrolipoamide dehydrogenase Homo sapiens 20-30 23339632-2 2013 Results showed that diaphorase (DP) and lactate dehydrogenases (LDH) had distinct binding selectivity and preference over reduced and oxidized states of coenzyme NAD(H). NAD 162-168 dihydrolipoamide dehydrogenase Homo sapiens 32-34 23339632-3 2013 On the basis of that, DP and LDH were chosen as indicator enzymes to distinguish the specific state of surface-bound NAD(H). NAD 117-123 dihydrolipoamide dehydrogenase Homo sapiens 22-24 22733276-7 2012 Together with two-photon imaging of NAD(P)H and confocal imaging of lipoamide dehydrogenase (LipDH) autofluorescence, we show that the ETC predominantly draws electrons from LipDH/NADH-dependent Complex I rather than from ETF/FADH(2)-dependent ETF:CoQ oxidoreductase (ETF-QO). NAD 180-184 dihydrolipoamide dehydrogenase Homo sapiens 68-91 22733276-7 2012 Together with two-photon imaging of NAD(P)H and confocal imaging of lipoamide dehydrogenase (LipDH) autofluorescence, we show that the ETC predominantly draws electrons from LipDH/NADH-dependent Complex I rather than from ETF/FADH(2)-dependent ETF:CoQ oxidoreductase (ETF-QO). NAD 180-184 dihydrolipoamide dehydrogenase Homo sapiens 93-98 22733276-7 2012 Together with two-photon imaging of NAD(P)H and confocal imaging of lipoamide dehydrogenase (LipDH) autofluorescence, we show that the ETC predominantly draws electrons from LipDH/NADH-dependent Complex I rather than from ETF/FADH(2)-dependent ETF:CoQ oxidoreductase (ETF-QO). NAD 180-184 dihydrolipoamide dehydrogenase Homo sapiens 174-179 20507824-7 2010 Then the oxidized state of DI was regenerated into its reduced native state by its natural substrate, nicotinamide adenine dinucleotide (NADH). NAD 137-141 dihydrolipoamide dehydrogenase Homo sapiens 27-29 19460292-7 2009 One of the identified proteins is dihydrolipoamide dehydrogenase (DLDH), a component of the alpha-ketoglutarate dehydrogenase (KGDH) complex, which uses NAD(+) as a substrate. NAD 153-159 dihydrolipoamide dehydrogenase Homo sapiens 34-64 19122206-4 2009 Both of the Fprs have a lower K(m) value for NADPH than for NADH in the diaphorase assays. NAD 60-64 dihydrolipoamide dehydrogenase Homo sapiens 72-82 19122206-5 2009 With NADH as electron donor, FprB also has a high specific constant (k(cat)/K(m)) in the diaphorase assay. NAD 5-9 dihydrolipoamide dehydrogenase Homo sapiens 89-99 19460292-7 2009 One of the identified proteins is dihydrolipoamide dehydrogenase (DLDH), a component of the alpha-ketoglutarate dehydrogenase (KGDH) complex, which uses NAD(+) as a substrate. NAD 153-159 dihydrolipoamide dehydrogenase Homo sapiens 66-70 16955758-3 2006 The method was based upon measurement of NADH generated from NAD+ during oxidation of bile acid by immobilized 3alpha-HSD with a color reagent consisting of nitrobluetetrazolium (NBT) chloride salt and immobilized diaphorase in 0.065 M sodium phosphate buffer (pH 7.0). NAD 61-65 dihydrolipoamide dehydrogenase Homo sapiens 214-224 18445470-7 2008 Subsequent action of glucose dehydrogenase (EC 1.1.1.47) and diaphorase (EC 1.6.99.2) in the presence of glucose and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl)-2H-tetrazolium (WST-1) acts to cycle the formed NAD between its oxidized and reduced forms, resulting in the production of WST-1 formazan, which is monitored at 450 nm. NAD 222-225 dihydrolipoamide dehydrogenase Homo sapiens 61-71 17395143-4 2007 The NAD is then amplified using an enzyme cycling system driven by glucose dehydrogenase and diaphorase. NAD 4-7 dihydrolipoamide dehydrogenase Homo sapiens 93-103 17175156-2 2007 The biosensor is based on the activity of glucose dehydrogenase (GDH) and diaphorase (DI) co-immobilized with NAD(+) into a carbon nanotube paste (CNTP) electrode modified with an osmium functionalized polymer. NAD 110-116 dihydrolipoamide dehydrogenase Homo sapiens 86-88 17175156-3 2007 This mediator was demonstrated to shuttle the electron transfer between the immobilized diaphorase and the CNTP electrode, thus, showing a good electrocatalytic activity towards NADH oxidation at potentials around +0.2V versus Ag AgCl, where interfering reactions are less prone to occur. NAD 178-182 dihydrolipoamide dehydrogenase Homo sapiens 88-98 17203264-4 2007 NADH is converted to NAD+ by applying hexacyanoferrate(III) as oxidant in the presence of DI. NAD 0-4 dihydrolipoamide dehydrogenase Homo sapiens 90-92 17203264-4 2007 NADH is converted to NAD+ by applying hexacyanoferrate(III) as oxidant in the presence of DI. NAD 21-25 dihydrolipoamide dehydrogenase Homo sapiens 90-92 16955758-3 2006 The method was based upon measurement of NADH generated from NAD+ during oxidation of bile acid by immobilized 3alpha-HSD with a color reagent consisting of nitrobluetetrazolium (NBT) chloride salt and immobilized diaphorase in 0.065 M sodium phosphate buffer (pH 7.0). NAD 41-45 dihydrolipoamide dehydrogenase Homo sapiens 214-224 19173061-6 2009 In the presence of the auxiliary enzyme DI, the PQI was reduced back to PAP and the resulting oxidized form of DI was finally regenerated in its reduced native state by its natural substrate, NADH. NAD 192-196 dihydrolipoamide dehydrogenase Homo sapiens 40-42 19173061-6 2009 In the presence of the auxiliary enzyme DI, the PQI was reduced back to PAP and the resulting oxidized form of DI was finally regenerated in its reduced native state by its natural substrate, NADH. NAD 192-196 dihydrolipoamide dehydrogenase Homo sapiens 111-113 17315258-1 2007 Mammalian mitochondrial dihydrolipoamide dehydrogenase (DLDH, EC 1.8.1.4) catalyzes NAD(+)-dependent oxidation of dihydrolipoamide in vivo and can also act as a diaphorase catalyzing in vitro nicotinamide adenine dinucleotide (reduced form) (NADH)-dependent reduction of electron-accepting molecules such as ubiquinone and nitroblue tetrazolium (NBT). NAD 84-90 dihydrolipoamide dehydrogenase Homo sapiens 56-60 17315258-1 2007 Mammalian mitochondrial dihydrolipoamide dehydrogenase (DLDH, EC 1.8.1.4) catalyzes NAD(+)-dependent oxidation of dihydrolipoamide in vivo and can also act as a diaphorase catalyzing in vitro nicotinamide adenine dinucleotide (reduced form) (NADH)-dependent reduction of electron-accepting molecules such as ubiquinone and nitroblue tetrazolium (NBT). NAD 192-225 dihydrolipoamide dehydrogenase Homo sapiens 56-60 17315258-1 2007 Mammalian mitochondrial dihydrolipoamide dehydrogenase (DLDH, EC 1.8.1.4) catalyzes NAD(+)-dependent oxidation of dihydrolipoamide in vivo and can also act as a diaphorase catalyzing in vitro nicotinamide adenine dinucleotide (reduced form) (NADH)-dependent reduction of electron-accepting molecules such as ubiquinone and nitroblue tetrazolium (NBT). NAD 242-246 dihydrolipoamide dehydrogenase Homo sapiens 56-60 17194138-2 2007 The approach was illustrated in the case of the bioelectrocatalytic oxidation of NADH by a diaphorase oxidoreductase in the presence of a ferrocene mediator. NAD 81-85 dihydrolipoamide dehydrogenase Homo sapiens 91-101 14695919-4 2003 The reduction of ubiquinone by lipoamide dehydrogenase and glutathione reductase is potently stimulated by zinc and the highest rate of reduction is achieved at acidic pH and the rates are equal with either NADPH or NADH as co-factors. NAD 216-220 dihydrolipoamide dehydrogenase Homo sapiens 31-54 15946682-3 2005 To catalyze the oxidation of dihydrolipoamide, hE3 uses two molecules: non-covalently bound FAD and a transiently bound substrate, NAD+. NAD 131-135 dihydrolipoamide dehydrogenase Homo sapiens 47-50 15946682-4 2005 To address the catalytic mechanism of hE3 and the structural basis for E3 deficiency, the crystal structures of hE3 in the presence of NAD+ or NADH have been determined at resolutions of 2.5A and 2.1A, respectively. NAD 135-139 dihydrolipoamide dehydrogenase Homo sapiens 112-115 15946682-4 2005 To address the catalytic mechanism of hE3 and the structural basis for E3 deficiency, the crystal structures of hE3 in the presence of NAD+ or NADH have been determined at resolutions of 2.5A and 2.1A, respectively. NAD 143-147 dihydrolipoamide dehydrogenase Homo sapiens 112-115 15946682-6 2005 The structure of oxidized hE3 with NAD+ bound demonstrates that the nicotinamide moiety is not proximal to the FAD. NAD 35-39 dihydrolipoamide dehydrogenase Homo sapiens 26-29 15946682-8 2005 This is the first time that this mechanistically requisite conformation of NAD+ or NADH has been observed in E3 from any species. NAD 75-79 dihydrolipoamide dehydrogenase Homo sapiens 109-111 15946682-8 2005 This is the first time that this mechanistically requisite conformation of NAD+ or NADH has been observed in E3 from any species. NAD 83-87 dihydrolipoamide dehydrogenase Homo sapiens 109-111 15946682-10 2005 The current hE3 structures show directly that the disease-causing mutations occur at three locations in the human enzyme: the dimer interface, the active site, and the FAD and NAD(+)-binding sites. NAD 176-182 dihydrolipoamide dehydrogenase Homo sapiens 12-15 15308223-3 2004 The resulting modified electrode was efficient for the ferricyanide-mediated NADH oxidation catalyzed by a diaphorase. NAD 77-81 dihydrolipoamide dehydrogenase Homo sapiens 107-117 15588129-2 2004 In the presence of NADH or NADPH, diaphorase can convert selected NO donors, glycerol trinitrate (GTN) and formaldoxime (FAL) to nitrites and nitrates with NO as an intermediate. NAD 19-23 dihydrolipoamide dehydrogenase Homo sapiens 34-44 15588129-8 2004 Reaction of FAL with diaphorase was lowered with SOD by 38 % indicating the partial participation of superoxide anion probably generated by the reaction of diaphorase with NADH or NADPH. NAD 172-176 dihydrolipoamide dehydrogenase Homo sapiens 21-31 15588129-8 2004 Reaction of FAL with diaphorase was lowered with SOD by 38 % indicating the partial participation of superoxide anion probably generated by the reaction of diaphorase with NADH or NADPH. NAD 172-176 dihydrolipoamide dehydrogenase Homo sapiens 156-166 15196936-0 2004 Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide. NAD 60-64 dihydrolipoamide dehydrogenase Homo sapiens 0-30 15196936-1 2004 Dihydrolipoamide dehydrogenase (DLDH; EC 1.8.1.4) from porcine heart is capable of using nitric oxide (NO) as an electron acceptor, with NADH as the electron donor, forming nitrate in the reaction. NAD 137-141 dihydrolipoamide dehydrogenase Homo sapiens 0-30 15196936-1 2004 Dihydrolipoamide dehydrogenase (DLDH; EC 1.8.1.4) from porcine heart is capable of using nitric oxide (NO) as an electron acceptor, with NADH as the electron donor, forming nitrate in the reaction. NAD 137-141 dihydrolipoamide dehydrogenase Homo sapiens 32-36 12117413-7 2002 The resultant NAD was amplified by a cycling assay involving alcohol dehydrogenase and diaphorase. NAD 14-17 dihydrolipoamide dehydrogenase Homo sapiens 87-97 11390211-5 2001 With the electrocatalytically reduced product, dihydrolipoic acid, lipoamide dehydrogenase could reduce NAD(+) in 20% yield and thioredoxin reductase NADP(+) in 18.4% yield. NAD 104-110 dihydrolipoamide dehydrogenase Homo sapiens 67-90 12200115-2 2002 The present study describes biotransformation of RDX via route 3 by a diaphorase (EC 1.8.1.4) from Clostridium kluyveri using NADH as electron donor. NAD 126-130 dihydrolipoamide dehydrogenase Homo sapiens 70-80 11772410-5 2002 The resultant NAD(+) can then be coupled to a cycling assay involving alcohol dehydrogenase and diaphorase. NAD 14-20 dihydrolipoamide dehydrogenase Homo sapiens 96-106 7619054-4 1995 The enzymes alcohol dehydrogenase and diaphorase are used to cycle beta-NAD+ in the presence of ethanol and p-Iodonitrotetrazolium Violet. NAD 67-76 dihydrolipoamide dehydrogenase Homo sapiens 38-48 9873629-1 1998 Electroenzymatic reduction of NAD+ to NADH for subsequent use in enzymatic synthesis has been carried out at carbon electrodes bearing lipoamide dehydrogenase (LiDH) immobilized under a Nafion film. NAD 30-34 dihydrolipoamide dehydrogenase Homo sapiens 135-158 9873629-1 1998 Electroenzymatic reduction of NAD+ to NADH for subsequent use in enzymatic synthesis has been carried out at carbon electrodes bearing lipoamide dehydrogenase (LiDH) immobilized under a Nafion film. NAD 30-34 dihydrolipoamide dehydrogenase Homo sapiens 160-164 9695367-3 1998 RESULTS: The cytochemical reaction for diaphorase/NADH revealed disorders of the mitochondrial activity and subtle and drastic malformations in the spermatozoa midpieces. NAD 50-54 dihydrolipoamide dehydrogenase Homo sapiens 39-49 8769129-4 1996 Under equivalent conditions at 20 degrees C, pH 8.0, mammalian TR reduced lipoic acid by NADPH 15 times more efficiently than the corresponding NADH dependent reduction catalyzed by LipDH (297 min-1 for TR vs. 20.3 min-1 for LipDH). NAD 144-148 dihydrolipoamide dehydrogenase Homo sapiens 182-187 8769129-6 1996 In contrast, LipDH was only 0.048 times as efficient in the forward reaction as compared to the reverse reaction (using NADH and NAD+). NAD 120-124 dihydrolipoamide dehydrogenase Homo sapiens 13-18 8769129-6 1996 In contrast, LipDH was only 0.048 times as efficient in the forward reaction as compared to the reverse reaction (using NADH and NAD+). NAD 129-133 dihydrolipoamide dehydrogenase Homo sapiens 13-18 18966494-6 1996 The diaphorase electrode thus obtained responds to NADH at 0 V. The sensitivity and detection limit of this biosensor are 11.2 mA M(-1) cm(-2) and 1 muM respectively. NAD 51-55 dihydrolipoamide dehydrogenase Homo sapiens 4-14 7499374-8 1995 It was found that NAD+ binding influences the interaction between the flavin and the reduced disulfide in the 2"-F-arabino-FAD-lipoamide dehydrogenase, presumably by altering the relative oxidation-reduction potentials. NAD 18-22 dihydrolipoamide dehydrogenase Homo sapiens 127-150 9873629-1 1998 Electroenzymatic reduction of NAD+ to NADH for subsequent use in enzymatic synthesis has been carried out at carbon electrodes bearing lipoamide dehydrogenase (LiDH) immobilized under a Nafion film. NAD 38-42 dihydrolipoamide dehydrogenase Homo sapiens 135-158 9873629-1 1998 Electroenzymatic reduction of NAD+ to NADH for subsequent use in enzymatic synthesis has been carried out at carbon electrodes bearing lipoamide dehydrogenase (LiDH) immobilized under a Nafion film. NAD 38-42 dihydrolipoamide dehydrogenase Homo sapiens 160-164 9378235-22 1997 Through the lipoamide dehydrogenase-dependent reduction of lipoic acid, the cell can draw on its NADH pool for antioxidant activity additionally to its NADPH pool, which is usually consumed during oxidative stress. NAD 97-101 dihydrolipoamide dehydrogenase Homo sapiens 12-35 8297331-3 1994 The study shows that microsomes contain NADH-dependent lipoamide reductase activity. NAD 40-44 dihydrolipoamide dehydrogenase Homo sapiens 55-74 7728971-9 1995 DES quinone was also reduced to DES by pure diaphorase, a mitochondrial reducing enzyme, in the presence of NADH. NAD 108-112 dihydrolipoamide dehydrogenase Homo sapiens 44-54 7822839-3 1994 The resulting NAD was measured by using a redox enzymatic recycling system of alcohol dehydrogenase, diaphorase and iodonitrotetrazolium as chromogen. NAD 14-17 dihydrolipoamide dehydrogenase Homo sapiens 101-111 7945680-2 1994 We show both photometrically by NADH+H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH+H+ catalyzed by porcine heart lipoamide dehydrogenase/diaphorase. NAD 32-36 dihydrolipoamide dehydrogenase Homo sapiens 157-180 7945680-2 1994 We show both photometrically by NADH+H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH+H+ catalyzed by porcine heart lipoamide dehydrogenase/diaphorase. NAD 32-36 dihydrolipoamide dehydrogenase Homo sapiens 181-191 7945680-2 1994 We show both photometrically by NADH+H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH+H+ catalyzed by porcine heart lipoamide dehydrogenase/diaphorase. NAD 122-126 dihydrolipoamide dehydrogenase Homo sapiens 157-180 7945680-2 1994 We show both photometrically by NADH+H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH+H+ catalyzed by porcine heart lipoamide dehydrogenase/diaphorase. NAD 122-126 dihydrolipoamide dehydrogenase Homo sapiens 181-191 8297331-9 1994 NADH/lipoamide-stimulated vitamin K epoxide reduction is uncoupled by traces of Triton X-100, suggesting that microsomal lipoamide reductase and vitamin K epoxide reductase are associated. NAD 0-4 dihydrolipoamide dehydrogenase Homo sapiens 121-140 8297331-10 1994 The results suggest that the vitamin K cycle obtains reducing equivalents from NADH through microsomal lipoamide reductase. NAD 79-83 dihydrolipoamide dehydrogenase Homo sapiens 103-122 1652585-1 1991 The oxidase reaction of lipoamide dehydrogenase with NADH generates superoxide radicals and hydrogen peroxide under aerobic conditions. NAD 53-57 dihydrolipoamide dehydrogenase Homo sapiens 24-47 1912072-6 1991 Thus, incubation of the alpha-ketoglutarate dehydrogenase complex with NADH has been found to induce the conversion from the non-cooperative form to the cooperative one, presumably through the reduction of lipoic acid bound to the complex in the reaction catalyzed by lipoyl dehydrogenase, the third component of the complex. NAD 71-75 dihydrolipoamide dehydrogenase Homo sapiens 268-288 1456954-4 1992 The role of flavin in the nitroreductase activity was supported by (a) the nitrofuran effect on the spectral properties of anaerobic, arsenite-inhibited, NADH-reduced LipDH; (b) FAD catalytic activity in a NADH-nitrofuran model system; and (c) the nitroreductase activity of LipDH monomer. NAD 154-158 dihydrolipoamide dehydrogenase Homo sapiens 167-172 1551239-2 1992 An enzymatic reaction involving alkaline phosphatase (EC 3.1.3.1) and galactose dehydrogenase (EC 1.1.1.48) produces NADH, which is coupled with diaphorase (EC 1.8.1.4) and iodonitrotetrazolium violet (INT). NAD 117-121 dihydrolipoamide dehydrogenase Homo sapiens 145-155 1751496-9 1991 Turnover in the dihydrolipoamide/NAD+ reaction is decreased by 10-fold and in the NADH/lipoamide reaction by 2-fold in I184Y lipoamide dehydrogenase. NAD 33-37 dihydrolipoamide dehydrogenase Homo sapiens 125-148 1751496-9 1991 Turnover in the dihydrolipoamide/NAD+ reaction is decreased by 10-fold and in the NADH/lipoamide reaction by 2-fold in I184Y lipoamide dehydrogenase. NAD 82-86 dihydrolipoamide dehydrogenase Homo sapiens 125-148 34164859-1 2021 Dihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin-dependent enzyme that catalyzes the NAD+ -dependent oxidation of dihydrolipoamide. NAD 98-102 dihydrolipoamide dehydrogenase Homo sapiens 0-30 1858346-4 1991 Apparent Ki value for NADH constituted 0.88-0.10 mM, thus demonstrating the effective regulation of the lipoamide dehydrogenase activity by end products. NAD 22-26 dihydrolipoamide dehydrogenase Homo sapiens 104-127 2173592-13 1990 The nitroreductase activity was inhibited by p-chloromercuribenzoate and enhanced by cadmium and arsenite, whereas the NADH-induced LADH inactivation failed to affect the nitroreductase activity. NAD 119-123 dihydrolipoamide dehydrogenase Homo sapiens 132-136 34164859-1 2021 Dihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin-dependent enzyme that catalyzes the NAD+ -dependent oxidation of dihydrolipoamide. NAD 98-102 dihydrolipoamide dehydrogenase Homo sapiens 32-36 2817348-5 1989 By stoichiometric coupling of this reaction with diaphorase/iodonitro tetrazolium chloride (INT) the formed NADH converts INT to a formazan whereby the reaction is displaced in favor of phenylpyruvate. NAD 108-112 dihydrolipoamide dehydrogenase Homo sapiens 49-59 2537814-5 1989 NADPH instead of NADH was the preferred electron donor of this lipoamide dehydrogenase. NAD 17-21 dihydrolipoamide dehydrogenase Homo sapiens 63-86 2736782-0 1989 Determination of NADH2-ferricyanide oxidoreductase (cytochrome b5 reductase, diaphorase) activity of human erythrocytes by an analysis of the time-dependence of NADH2 oxidation. NAD 17-22 dihydrolipoamide dehydrogenase Homo sapiens 77-87 2736782-1 1989 The time-dependence of the reaction of human erythrocyte diaphorase activity has been studied by the use of NADH2 and ferricyanide as substrates. NAD 108-113 dihydrolipoamide dehydrogenase Homo sapiens 57-67 2736782-3 1989 These findings indicate that human erythrocyte diaphorase has a Km value for NADH2 by far higher than, and for ferricyanide by far lower than, the concentration of the substrates used, i.e. 0.1 and 0.2 mmol/l, respectively. NAD 77-82 dihydrolipoamide dehydrogenase Homo sapiens 47-57 2736782-5 1989 Diaphorase activity was found to be 7.29 +/- 3.69 1 SD mumol NADH2 oxidized/ml packed cells per min, at 25 degrees C, and pH 7.00. NAD 61-66 dihydrolipoamide dehydrogenase Homo sapiens 0-10 3047261-1 1988 Enzyme-amplified immunoassays have been adapted for electrochemical measurement, using an NAD+/NADH redox cycle coupled to an electrode via the active site of diaphorase. NAD 90-94 dihydrolipoamide dehydrogenase Homo sapiens 159-169 6719320-0 1984 [Congenital deficiency of erythrocyte NADH-dependent methemoglobin reductase (diaphorase)]. NAD 38-42 dihydrolipoamide dehydrogenase Homo sapiens 78-88 3662051-1 1987 Investigations were carried out into the activity and localization of NADH-dependant diaphorase in boar spermatozoa. NAD 70-74 dihydrolipoamide dehydrogenase Homo sapiens 85-95 3576723-1 1987 Lipoamide dehydrogenase (EC 1.6.4.3) from the ketoglutarate dehydrogenase complex of adrenals catalyzes the oxidation of NADH by lipoamide and quinone compounds according to the "ping-pong" scheme. NAD 121-125 dihydrolipoamide dehydrogenase Homo sapiens 0-23 3576723-6 1987 The patterns of NAD+ inhibition in the quinone reductase reaction differ from that of lipoamide reductase reaction. NAD 16-20 dihydrolipoamide dehydrogenase Homo sapiens 86-105 3732277-10 1986 Diaphorase was used to couple the oxidation of NADH to the production of duroquinol which acted as electron donor to nitrate reductase. NAD 47-51 dihydrolipoamide dehydrogenase Homo sapiens 0-10 3512723-3 1986 First, NADP is dephosphorylated to produce NAD, which catalytically activates a specific redox-cycle involving the enzymes alcohol dehydrogenase and diaphorase. NAD 7-10 dihydrolipoamide dehydrogenase Homo sapiens 149-159 3754027-2 1986 Formate is oxidized by formate dehydrogenase producing NADH which reduces INT via diaphorase to a visible red-colored endpoint that can be measured on a spectrophotometer at 500 nm. NAD 55-59 dihydrolipoamide dehydrogenase Homo sapiens 82-92 3593260-2 1987 In the presence of NADH, lipoamide dehydrogenase reduces the nitro group of 4-nitropyridine and 4-nitropyridine N-oxide. NAD 19-23 dihydrolipoamide dehydrogenase Homo sapiens 25-48 18553714-6 1985 NADH regeneration activity based on malic acid production rate was 4.7 U/mg of the enzyme protein of the commercial diaphorase preparation. NAD 0-4 dihydrolipoamide dehydrogenase Homo sapiens 116-126 6546954-5 1984 Under physiological conditions, lipoamide dehydrogenase and glutathione reductase act in opposite directions, passing reducing equivalents to NAD+ or from NADPH (respectively), and two key substitutions near the redox centre could be associated with this difference in function. NAD 142-146 dihydrolipoamide dehydrogenase Homo sapiens 32-55 6895053-3 1981 The hydrogen in the NADH generated is transferred by diaphorase (EC 1.6.4.3) to nitrotetrazolium blue to yield diformazan 540 nm). NAD 20-24 dihydrolipoamide dehydrogenase Homo sapiens 53-63 7060551-10 1982 The structure of the NADPH domain is probably homologous with the NAD domain of lipoamide dehydrogenase and with the FAD domain of several proteins, but not with NADPH domains of known chain-fold in other proteins. NAD 21-24 dihydrolipoamide dehydrogenase Homo sapiens 80-103 6340103-4 1983 By using a third enzyme, lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3), which was also coupled to the same beads and which competes with lactate dehydrogenase for the NADH produced by alcohol dehydrogenase, the effect of site-to-site directed immobilization was studied. NAD 50-54 dihydrolipoamide dehydrogenase Homo sapiens 25-48 4284825-0 1965 A kinetic study of the lipoamide dehydrogenase-NADH-dye reaction. NAD 47-51 dihydrolipoamide dehydrogenase Homo sapiens 23-46 7193456-11 1980 The Km for NAD+ is 0.7 mM for both the complex and the lipoamide dehydrogenase. NAD 11-15 dihydrolipoamide dehydrogenase Homo sapiens 55-78 7193456-13 1980 The lipoamide dehydrogenase is inhibited by NADH and NADPH competitively with NAD+, with Ki values of 80 and 90 microM respectively. NAD 44-48 dihydrolipoamide dehydrogenase Homo sapiens 4-27 7193456-13 1980 The lipoamide dehydrogenase is inhibited by NADH and NADPH competitively with NAD+, with Ki values of 80 and 90 microM respectively. NAD 78-82 dihydrolipoamide dehydrogenase Homo sapiens 4-27 507807-0 1979 Purification of lipoamide dehydrogenase from Ascaris muscle mitochondria and its relationship to NADH:NAD+ transhydrogenase activity. NAD 97-101 dihydrolipoamide dehydrogenase Homo sapiens 16-39 454630-3 1979 Lipoyl dehydrogenase (NADH:lipoamide oxidereductase, EC 1.6.4.3), DT-diaphorase (NAD(P)H:(quinone-acceptor) oxidoreductase, EC 1.6.99.2) and liver microsomes could also catalyze the conversion of cis-3-(5-nitro-2-furyl)-2-(2-furyl)acrylamide to its trans isomer in the presence of an appropriate electron donor. NAD 22-26 dihydrolipoamide dehydrogenase Homo sapiens 0-20 13996531-0 1963 A new NAD-dependent spectral species of lipoamide dehydrogenase. NAD 6-9 dihydrolipoamide dehydrogenase Homo sapiens 40-63 657494-4 1978 The hydrogen in the generated NADH is transferred by diaphorase (EC 1.6.4.3) to resazurin to yield resorfin, the fluorophore. NAD 30-34 dihydrolipoamide dehydrogenase Homo sapiens 53-63 1125255-7 1975 Reduction of alpha-lipoic cid with NADH by lipoyl dehydrogenase was activated by NAD, but that of asparagusic acid by asparagusate dehydrogenase was inactivated by NAD. NAD 35-39 dihydrolipoamide dehydrogenase Homo sapiens 43-63 1125255-7 1975 Reduction of alpha-lipoic cid with NADH by lipoyl dehydrogenase was activated by NAD, but that of asparagusic acid by asparagusate dehydrogenase was inactivated by NAD. NAD 35-38 dihydrolipoamide dehydrogenase Homo sapiens 43-63 1125255-7 1975 Reduction of alpha-lipoic cid with NADH by lipoyl dehydrogenase was activated by NAD, but that of asparagusic acid by asparagusate dehydrogenase was inactivated by NAD. NAD 81-84 dihydrolipoamide dehydrogenase Homo sapiens 43-63 32286819-6 2020 Diaphorase (DH) was immobilized by a cobaltocene-modified poly(allylamine) redox polymer on the electrode surface (DH/Cc-PAA bioelectrode) to achieve effective bioelectrocatalytic NADH regeneration. NAD 180-184 dihydrolipoamide dehydrogenase Homo sapiens 0-10 28617502-1 2017 Diaphorase and a benzylpropylviologen redox polymer were combined to create a bioelectrode that can both oxidize NADH and reduce NAD+. NAD 113-117 dihydrolipoamide dehydrogenase Homo sapiens 0-10 28617502-1 2017 Diaphorase and a benzylpropylviologen redox polymer were combined to create a bioelectrode that can both oxidize NADH and reduce NAD+. NAD 129-133 dihydrolipoamide dehydrogenase Homo sapiens 0-10 25757537-0 2015 Conformational Change Near the Redox Center of Dihydrolipoamide Dehydrogenase Induced by NAD(+) to Regulate the Enzyme Activity. NAD 89-95 dihydrolipoamide dehydrogenase Homo sapiens 47-77 25757537-1 2015 Dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide (DHL) to NAD(+) mediated by FAD. NAD 94-100 dihydrolipoamide dehydrogenase Homo sapiens 0-30 27078679-3 2016 In this study, we discuss these interference challenges and highlight the specific case of the diaphorase/resazurin system that can be coupled to enzymes utilizing NADH or NADPH. NAD 164-168 dihydrolipoamide dehydrogenase Homo sapiens 95-105