Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glycosomes and mitochondrial vesicles from cultured promastigotes of Leishmania mexicana mexicana have been separated using isopycnic centrifugation on linear sucrose gradients. Hexokinase (EC 2.7.1.2), glucose phosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), and phosphoenolpyruvate carboxykinase (EC 4.1.1.49) were recovered largely in association with glycosomes (density; 1.215 g/ml). Phosphoglycerate kinase (EC 2.7.2.3) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) had some small glycosomal activity, but were mostly recovered in the soluble fractions. Malate dehydrogenase (EC 1.1.1.37) showed a broad peak corresponding to that of the mitochondrial marker oligomycin-sensitive ATPase (EC 3.6.1.4) (density; 1.190 g/ml). Glutamate dehydrogenase (EC 1.4.1.3) and alanine aminotransferase (EC 2.6.1.2) both showed small mitochondrial peaks, but most of the activities were recovered elsewhere on the gradient and in the soluble fractions. The subcellular location of enzymes in L.m. mexicana amastigotes was investigated by following the release of soluble enzymes from digitonin-treated amastigotes. This revealed distinct cytosolic, mitochondrial, and glycosomal compartments. The findings give an insight into the organization and control of L.m. mexicana promastigote and amastigote energy metabolism.
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PMID:Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes. 315 38

Tobacco smoke absorbed in phosphate buffer at neutral pH inhibits irreversibly the enzymes rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and yeast alcohol dehydrogenase, whereas lactic dehydrogenase and glutamic dehydrogenase are not inhibited. A transient inhibition of beef liver catalase occurs. Indirect evidence suggests that the observed enzyme inhibition is caused by peroxides present in the smoke.
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PMID:Inhibiting effect of tobacco smoke on some crystalline enzymes. 1375 16

Burchall, J. J. (University of Illinois, Urbana), R. A. Niederman, and M. J. Wolin. Amino group formation and glutamate synthesis in Streptococcus bovis. J. Bacteriol. 88:1038-1044. 1964.-Extracts of Streptococcus bovis grown on NH(4) (+) as a nitrogen source contain a nicotinamide adenine dinucleotide phosphate (NADP)-linked glutamic dehydrogenase and are devoid of alanine dehydrogenase, other amino acid dehydrohygenases, and aspartase. A potential source of reduced nicotinamide adenine dinucleotide phosphate for glutamate synthesis is a NADP and nicotinamide adenine dinucleotide (NAD)-linked glyceraldehyde-3-phosphate dehydrogenase present in the extracts. Experiments with C(14)-labeled glucose and NaHCO(3) indicate that the glutamate carbon skeleton is synthesized by a tricarboxylic acid pathway. The synthesis of the carbon skeleton of glutamate is repressed when glutamate or casein hydrolysate supplement the NH(4) (+)-containing growth medium. Repression of glutamic dehydrogenase and a NAD-linked isocitric dehydrogenase occurs only when complex nitrogen sources, but not when free amino acids, are added to the growth medium.
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PMID:AMINO GROUP FORMATION AND GLUTAMATE SYNTHESIS IN STREPTOCOCCUS BOVIS. 1421 16