PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27908734-2 2017 Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism. d-glyceraldehyde 3-phosphate 113-141 triosephosphate isomerase 1 Homo sapiens 0-27 28990791-1 2017 Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate. d-glyceraldehyde 3-phosphate 108-136 triosephosphate isomerase 1 Homo sapiens 0-25 28990791-1 2017 Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP), via an enediol(ate) intermediate. d-glyceraldehyde 3-phosphate 108-136 triosephosphate isomerase 1 Homo sapiens 27-30 27908734-2 2017 Triosephosphate isomerase 1 (TPI1), which catalyzes the interconversion of dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde-3-phosphate (G3P) during glycosis and gluconeogenesis, is a crucial enzyme in the carbohydrate metabolism. d-glyceraldehyde 3-phosphate 113-141 triosephosphate isomerase 1 Homo sapiens 29-33 11419952-1 2001 Product release is partially rate determining in the isomerization reaction catalyzed by Triosephosphate Isomerase, the conversion of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, probably because an active-site loop movement is necessary to free the product from confinement in the active-site. d-glyceraldehyde 3-phosphate 164-192 triosephosphate isomerase 1 Homo sapiens 89-114 21995300-1 2011 D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively. d-glyceraldehyde 3-phosphate 127-155 triosephosphate isomerase 1 Homo sapiens 0-53 21995300-1 2011 D-Xylose isomerase (XI) and triosephosphate isomerase (TIM) catalyze the aldose-ketose isomerization reactions of D-xylose and d-glyceraldehyde 3-phosphate (DGAP), respectively. d-glyceraldehyde 3-phosphate 127-155 triosephosphate isomerase 1 Homo sapiens 55-58 18175010-1 2008 The catalytic base at the active site of triosephosphate isomerase (TIM) was labelled with -H by abstraction of a proton from substrate d-glyceraldehyde 3-phosphate to form an enzyme-bound enediol(ate) in D2O solvent. d-glyceraldehyde 3-phosphate 136-164 triosephosphate isomerase 1 Homo sapiens 41-66 18175010-1 2008 The catalytic base at the active site of triosephosphate isomerase (TIM) was labelled with -H by abstraction of a proton from substrate d-glyceraldehyde 3-phosphate to form an enzyme-bound enediol(ate) in D2O solvent. d-glyceraldehyde 3-phosphate 136-164 triosephosphate isomerase 1 Homo sapiens 68-71 29123462-2 2015 Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis. d-glyceraldehyde 3-phosphate 74-102 triosephosphate isomerase 1 Homo sapiens 0-25 29123462-2 2015 Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis. d-glyceraldehyde 3-phosphate 74-102 triosephosphate isomerase 1 Homo sapiens 27-30 25092608-2 2014 The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP). d-glyceraldehyde 3-phosphate 307-335 triosephosphate isomerase 1 Homo sapiens 61-64 25092608-2 2014 The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an alpha-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or d-glyceraldehyde 3-phosphate (DGAP). d-glyceraldehyde 3-phosphate 307-335 triosephosphate isomerase 1 Homo sapiens 75-100 23505326-3 2011 Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation. d-glyceraldehyde 3-phosphate 61-89 triosephosphate isomerase 1 Homo sapiens 0-25 23505326-3 2011 Triosephosphate isomerase (TIM) catalyzed interconversion of D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate is being studied as a prototype for enzyme catalyzed proton transfer, and orotidine monophosphate decarboxylase (OMPDC) catalyzed decarboxylation of orotidine 5"-monophosphate is being studied as a prototype for enzyme-catalyzed decarboxylation. d-glyceraldehyde 3-phosphate 61-89 triosephosphate isomerase 1 Homo sapiens 27-30 8841131-2 1996 Secondary kH/kT kinetic isotope effects in H2O and kH/kT or kD/kT isotope effects in D2O have been measured for the triosephosphate isomerase-catalyzed conversion of dihydroxyacetone 3-phosphate (DHAP) to D-glyceraldehyde 3-phosphate. d-glyceraldehyde 3-phosphate 205-233 triosephosphate isomerase 1 Homo sapiens 116-141 11151009-3 2001 The tight phosphate-binding pocket explains the high substrate specificity of TIM being limited to the in vivo substrates dihydroxyacetone-phosphate and D-glyceraldehyde-3-phosphate. d-glyceraldehyde 3-phosphate 153-181 triosephosphate isomerase 1 Homo sapiens 78-81 2043623-1 1991 The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (GAP) at a rate limited by the diffusion of substrate to the enzyme. d-glyceraldehyde 3-phosphate 149-177 triosephosphate isomerase 1 Homo sapiens 49-52 1290934-1 1992 A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM). d-glyceraldehyde 3-phosphate 102-130 triosephosphate isomerase 1 Homo sapiens 160-186 1290934-1 1992 A theoretical approach is employed to study the catalysis of the dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde 3-phosphate (GAP) reaction by the enzyme triose phosphate isomerase (TIM). d-glyceraldehyde 3-phosphate 102-130 triosephosphate isomerase 1 Homo sapiens 188-191 999835-1 1976 When the isomerization of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and the product become labeled. d-glyceraldehyde 3-phosphate 26-54 triosephosphate isomerase 1 Homo sapiens 101-126 6446532-4 1980 The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triosephosphate isomerase. d-glyceraldehyde 3-phosphate 60-88 triosephosphate isomerase 1 Homo sapiens 117-142 999834-1 1976 When the isomerization of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate is catalyzed by triosephosphate isomerase in tritiated water, both the substrate and product become labeled. d-glyceraldehyde 3-phosphate 56-84 triosephosphate isomerase 1 Homo sapiens 101-126 2417997-4 1985 The dihydroxyacetone phosphate is reversibly converted into D-glyceraldehyde-3-phosphate by exogenous and endogenous triose phosphate isomerase. d-glyceraldehyde 3-phosphate 60-88 triosephosphate isomerase 1 Homo sapiens 117-143 999837-1 1976 The isomerization of specifically deuterium-labeled [1(R)-2H5dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate, catalyzed by the enzyme triosephosphate isomerase, has been studied. d-glyceraldehyde 3-phosphate 91-119 triosephosphate isomerase 1 Homo sapiens 145-170 999838-1 1976 The experimental results on the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate catalyzed by triosephosphate isomerase that are presented in the previous five papers are here collected and analyzed according to the theory presented in the first paper (Albery, W.J., Knowles, J.R. (1976), Biochemistry 15, the first of eight papers in a series in this issue). d-glyceraldehyde 3-phosphate 82-110 triosephosphate isomerase 1 Homo sapiens 124-149 4309306-0 1969 The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase. d-glyceraldehyde 3-phosphate 29-57 triosephosphate isomerase 1 Homo sapiens 137-163 4309306-6 1969 Aldolase and triose phosphate isomerase both liberate d-glyceraldehyde 3-phosphate as the aldehyde. d-glyceraldehyde 3-phosphate 54-82 triosephosphate isomerase 1 Homo sapiens 13-39