Human, glyceraldehyde-3-phosphate

Ercolani, L., Florence, B., Denaro, M., Alexander, M. (1988). Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene. J. Biol. Chem. 263, 15335-15341. 

C. Lind, R. Gerdes, I. Schuppe-Koistinen, and LA. Cotgreave, Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione catalysis by glutaredoxin, Biochem. Biophys. Res. Commun. 247 (1998) 481-486. 

Welch JE, Brown PL, O Brien DA, et al. Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J Androl 2000 21 328-338. 

Disch A, Schwender J, Muller C, Lichtenthaler HK, Rohmer M (1998) Distribution of the meval-onate and glyceraldehyde phosphate/pyruvate pathways for isoprenoid biosynthesis in unicellular algae and the cyanobacterium Synechocystis PCC 6714. Biochem J 333 381-388 Dittmann E, Wiegand C (2006) Cyanobacterial toxins - occurrence, biosynthesis and impact on human affairs. Mol Nutr Food Res 50 7-17... 

Enzymes with niacin coenzymes in human metabolism (examples of 200 enzymes ). L-Lactate dehydrogenase (EC 1.1.1.27) alcohol dehydrogenase (EC l.l.l.l) glyceraldehyde-phosphate dehydrogenase (EC 1.2.1.12) NADPH-cytochrome-P-450-reductase (EC 1.6.2.4). 

Variations in amount of RNA loaded per lane is determined by probing the blot with a human cDNA probe for glyceraldehyde phosphate dehydrogenase (GAPDH) (obtained from ATCC). 

The hexose phosphate, fructose-1,6-diphosphate, is split by aldolase into two triose phosphates glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. Aldolase consists of four 40-kDa subunits. Three tissue-specific forms exist in human tissues aldolase A (ubiquitous and very active in the muscle), aldolase B (liver, kidney, and small intestine), and aldolase C (specific to the brain). These three isozymes have nearly the same molecular size but differ in substrate specificity,... 

Among the specific enzymes whose activity has been reported to be decreased after in vitro ozone exposure are papain, glyceraldehyde-3-phosphate dehydrogenase, lysozyme, ribonuclease, and acetylcholinesterase. The latter enzyme appears to be particulady susceptible to free-radical and oxidative states. A loss in acetylcholinesterase activity has been reported in the red cells of humans and mice that inhaled ozone. However, there are only minimal amounts of this enzyme in lupg tissue, and, although it has been suggested that acetylcholinesterase is important in bronchial tract ciliary activity, there is no direct evidence to support this conjecture. 

Outline in detail, using structural formulas, the enzyme-catalyzed reactions by which cells in the human body convert glyceraldehyde 3-phosphate into pyruvate. 

Gregus, Z. and Nemeti, B. (2005) The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase works as an arsenate reductase in human red blood cells and rat liver cytosol. Toxicological Sciences, 85(2), 859-69. 

Like transketolase, transaldolase (TA, E.C. 2.2.1.2) is an enzyme in the oxidative pentose phosphate pathway. TA is a class one lyase that operates through a Schiff-base intermediate and catalyzes the transfer of the C(l)-C(3) aldol unit from D-sedoheptulose 7-phosphate to glyceraldehyde-3-phosphate (G3P) to produce D-Fru 6-P and D-erythrose 4-phosphate (Scheme 5.59). TA from human as well as microbial sources have been cloned.110 111 The crystal structure of the E. coliu and human112 transaldolases have been reported and its similarity to the aldolases is apparent, since it consists of an eight-stranded (o /(3)s or TIM barrel domain as is common to the aldolases. As well, the active site lysine residue that forms a Schiff base with the substrate was identified.14112 Thus, both structurally and mechanistically it is related to the type I class of aldolases. 

Hoshi K, Nomura K, Sano Y, and Koshihara Y (1999) Nuclear vitamin K2 binding protein in human osteoblasts homologue to glyceraldehyde-3-phosphate dehydrogenase. Biochemical Pharmacology 58,1631-8. 

I. Schuppe-Koistinen, P. Moldeus, T. Bergman, and I.A. Cotgreave, S-Thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment, Eur. J Biochem. 221 (1994) 1033-1037. 

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