Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The inhibition of D-glyceraldehyde-3-phosphate dehydrogenase by ATP is of purely mixed type with respect to NAD (Ki=4.9 mM), purely uncompetitive with respect to D-glyceraldehyde-3-phosphate (Ki=9.4 mM) and partially uncompetitive with respect to inorganic phosphate (Ki=6.0 mM). Quinaldate is a purely mixed type inhibitor with respect to both NAD (Ki==10.0 mM) and D-glyceraldehyde-3-phosphate (Ki=15.3 mM), whereas purely non-competitive with respect to inorganic phosphate (Ki=11.0 mM). In the presence of quinaldate a lag period is observed in the time course of enzyme reaction. The duration of this lag period depends on both quinaldate and substrate concentrations.
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PMID:Inhibition of D-glyceraldehyde-3-phosphate dehydrogenase by ATP and quinaldate. 51 4

The simultaneous action of ATP (partially uncompetitive inhibitor with respect to Pi) and quinaldate (purely non-competitive inhibitor with respect to Pi) on D-glyceraldehyde-3-phosphate dehydrogenase was analyzed kinetically. The interaction constant [as defined by Keleti and Fajszi (1971) Math. Biosci. 12 197] of the two inhibitors for the D-glyceraldehyde-3-phosphate dehydrogenase-Pi complex is greater than 1, which means that the two inhibitors act antagonistically. The kinetic analysis of the double inhibition shows that there is no ATP-enzyme-quinaldate ternary complex, but a quaternary complex with Pi is formed. The interaction of the two inhibitors on the enzyme-Pi complex depends on substrate (Pi) concentration. The antagonistic effect of the two inhibitors becomes additive at low Pi concentrations (about 1 mM). The simultaneous action of oxalate (purely uncompetitive inhibitor with respect to NAD) and quinaldate (partially mixed type inhibitor with respect to NAD) on lactate dehydrogenase was also analyzed. Oxalate and quinaldate act antagonistically on lactate dehydrogenase. However, at low NAD concentrations (about 0.06 mM) or at high quinaldate and low oxalate concentrations (around 7 and 1.7 mM, respectively) the antagonism turns into the simple summation of the effects of the two inhibitors.
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PMID:Double inhibition of D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase. 51 6

In biopsy samples of the lateral part of the quadriceps femoris muscle of 6 obese diabetic male patients and of 11 obese males with a normal glucose tolerance, the activities of 7 enzymes of energy metabolism were estimated: hexokinase, cytoplasmic glycerol-3-phosphate: NAD dehydrogenase, triosephosphate dehydrogenase, lactate dehydrogenase, citrate synthase, malate dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase. The obese diabetic male patients exhibited decreased activities of enzymes of carbohydrate breakdown and cytoplasmic NAD regeneration. Enzymes connected functionally with aerobic metabolism were less affected. The unchanged activity of 3-hydroxyacyl-CoA dehydrogenase points to an increased role of fatty acid catabolism in the muscle.
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PMID:Enzyme activities in quadriceps femoris muscle of obese diabetic male patients. 90 76

1. In 3 groups of men, differing as to the amount and intensity of physical training loads, increasing in the order "sedentary": "sporting": "athletic", enzyme activities were estimated in biopsy samples of m. quadriceps femoris (vastus lateralis). The enzymes were: Hexokinase (HK), NAD: glycerol-3-phosphate dehydrogenase (GPDH), triosephosphate dehydrogenase (TPDH), lactate dehydrogenase (LDH), citrate synthase (CS), NAD: malate dehydrogenase (MDH), and 3-hydroxyacyl-CoA dehydrogenase (HOADH). Indicators of laboratory performance and whole-body metabolic capacities (maximal oxygen consumption etc.) were estimated in the "sporting" and "athletic" groups. 2. In the 2 latter groups, distinguished by greater physical activity, the atypical enzyme activity pattern, remarkable by a low activity of LDH and high relative activities of GPDH and HK, as reported earlier in a sedentary group (Bass et al., 1975a), disappeared. The possibility of the atypical low LDH enzyme activity pattern as resulting from lack of bodily exertion is discussed. 3. The moderately trained "sporting" group distinguishes itself from the "sedentary" one mainly by a higher activity of LDH and by lower activities of GPDH and MDH. In the intensively trained "athletic" group, enzymes connected to aerobic oxidation (MDH, CS, HOADH) and GPDH also show higher activities than in the "sporting" group. The difference between the two more active groups is further borne out by a higher maximum oxygen uptake and carbon dioxide release of the well-trained "athletic" group. This difference of enzyme activity pattern may not be confined to the quadriceps femoris muscle.
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PMID:Enzyme activity patterns of energy supplying metabolism in the quadriceps femoris muscle (vastus lateralis): sedentary men and physically active men of different performance levels. 94 91

The amino acid sequences of pig muscle and of yeast glyceraldehyde-3-phosphate dehydrogenase are compared with the three-dimensional structure of the lobster muscle enzyme. Residues in sheet and helical regions, on the exterior and interior, in subunit and domain interfaces, as well as residues in the active site have been examined for evolutionary conservation. The residues in the first (NAD binding) domain (1-147) are less conserved than residues in the second (catalytic) domain (148-334) probably because there are fewer internal residues and fewer residues involved in interactions between subunits. Residues in subunit interface are conserved to a significantly greater extent than others, and those involved in catalysis are conserved most of all. Patterns of residues in helices and sheets follow those found for other proteins.
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PMID:Sequence variability and structure of D-glyceraldehyde-3-phosphate dehydrogenase. 110 21

1. The following enzyme activities were estimated in needle-biopsy samples of the lateral part of the human quadriceps femoris muscle: triosephosphate dehydrogenase (TPDH), lactate dehydrogenase (LDH), NAD : glycerol-3-phosphate dehydrogenase (GPDH), hexokinase (HK), NAD: malate dehydrogenase (MDH), citrate synthase (CS) and hydroxyacyl-CoA dehydrogenase. 2. Although the enzyme activities in muscles of women were lesser than in those of men, no difference was found in the calculated enzyme activity ratios. There is thus no sex-dependent metabolic type-differentiation in this muscle. 3. The human quadriceps femoris is a low-activity muscle, in comparison with muscles of homoiotherm laboratory animals. The enzyme activity ratio of TPDH to CS, characterizing the glycolytic pyruvate formation to aerobic oxidative capacities, shows this muscle to be of an intermediate type in this respect, similarly as the extensor digitorum longus of the rat. The relatively very high capacity of glucose phosphorylation (HK), the high aerobic regeneration of cytoplasmic dehydrogenated NAD (GPDH) and the very low anaerobic regeneration (LDH), show the unusually high proportion of carbohydrates (glucose) which can be broken down aerobically.
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PMID:M. Quadriceps femoris of man, a muscle with an unusual enzyme activity pattern of energy supplying metabolism in mammals. 116 80

1. In biopsy samples of the lateral part of m. quadriceps femoris of 49 obese and 14 lean persons the activities of the following enzymes were investigated: triosephosphate dehydrogenase (TPDH), glycerolphosphate: nad dehydrogenase (GPDH), lactate dehydrogenase (LDH), hexokinase (HK), malate: NAD dehydrogenase (MDH), citrate synthase (CS) and hydroxyacyl-CoA dehydrogenase (HOADH). 2. The muscles of obese had an increased activity ratio of TPDH to CS and to HK, respectively, caused in muscles of female obese subjects by an increase of TPDH activity, in those of obese men rather by a decrease of CS and HK activities. 3. Cluster analysis brough to light the existence of three major groups. Group 1 (low activity-low LDH group), consisting of muscles of female obese subjects only, exhibited low activities of all enzymes investigated, that of LDH being so low as to possibly induce a serious deficiency of anerobic metabolism under working conditions. Group 2 (medium enzyme activity group) was characterized by medium enzyme activities, similar to that of lean controls (included in this group). This consisted of subjects of both sex. Group 3 (high enzyme activity group) consisted of obese of both sex. It was distinguished by high enzyme activities, especially of LDH. It is suggested that the groups of similar enzyme activity patterns might reflect different stages, types and/or genesis of obesity.
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PMID:Metabolic changes in the quadriceps femoris muscle of obese people. Enzyme activity patterns of energy-supplying metabolism. 123 24

Nitric oxide generation in brain cytosolic fractions markedly enhances ADP-ribosylation of a single 37-kDa protein. By utilizing a biotinylated NAD and avidin affinity chromatography, we purified this protein. Partial amino acid sequencing establishes its identity as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This is further confirmed by detection of GAPDH enzymatic activity in the purified 37-kDa protein. GAPDH is ADP-ribosylated in the absence of brain extract. This auto-ADP-ribosylation is enhanced by nitric oxide generation. ADP-ribosylation appears to involve the cysteine where NAD interacts with GAPDH so that ADP-ribosylation likely inhibits enzymatic activity. Such inhibition may play a role in nitric oxide-mediated neurotoxicity.
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PMID:Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. 140 44

Auto-ADP-ribosylation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GraPDH) has recently been demonstrated to be dramatically stimulated in the presence of nitric oxide. In order to obtain insight into the sequence of events leading to ADP-ribosylation of GraPDH, we studied the target amino acid, the nucleotide cofactor requirement, pH dependency and the stoichiometry of the reaction. Basal as well as stimulated ADP-ribose transfer is inhibited by the SH-group alkylating reagent, N-ethylmaleimide. Furthermore, the radiolabel of auto-[32P]ADP-ribosylated GraPDH is removed by treatment with HgCl2, suggesting an ADP-ribose-cysteine bond. Several indirect and direct mechanistic considerations point to NAD+ as the only cofactor for the ADP-ribosylation reaction, excluding the possibility of a reaction sequence involving a NAD-glycohydrolase(s) followed by nonenzymatic ADP-ribose transfer to GraPDH. Optimal ADP-ribosylations were carried out at alkaline pH values using 10 microM free NAD+ as the sole nucleotide cofactor. Bovine serum albumin with an S-nitrosylated SH group can serve as a model of ADP-ribose transfer from NAD+ and suggests that the nitric-oxide-modified SH group (S-nitrosylated SH group) is a prerequisite for the reaction.
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PMID:Characterization of a nitric-oxide-catalysed ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. 144 79

NAD(P) aldehyde dehydrogenases (EC 1.2.1.3) are a family of enzymes that oxidize a wide variety of aldehydes into acid or activated acid compounds. Using site-directed mutagenesis, the essential nucleophilic Cys 149 in the NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Escherichia coli has been replaced by alanine. Not unexpectedly, the resulting mutant no longer shows any oxidoreduction phosphorylating activity. The same mutation, however, endows the enzyme with a novel oxidoreduction nonphosphorylating activity, converting glyceraldehyde 3-phosphate into 3-phosphoglycerate. Our study further provides evidence for an alternative mechanism in which the true substrate is the gem-diol entity instead of the aldehyde form. This implies that no acylenzyme intermediate is formed during the catalytic event. Therefore, the mutant C149A is a new enzyme which catalyzes a distinct reaction with a chemical mechanism different from that of its parent phosphorylating glyceraldehyde-3-phosphate dehydrogenase. This finding demonstrates the possibility of an alternative route for the chemical reaction catalyzed by classical nonphosphorylating aldehyde dehydrogenases.
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PMID:A new chemical mechanism catalyzed by a mutated aldehyde dehydrogenase. 146 40


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