Human glyceraldehyde-3-phosphate dehydrogenase

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). 

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. 

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. 

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. 

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. 

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. 

Comparative studies on proteins from different species show that the structures are essentially the same despite different crystallisation conditions. Examples include sperm whale and seal myoglobin, horse and human haemoglobin, horse, tuna, bonito and rice cytochrome c, hen egg white, tortoise egg white and human lysozyme, horse and yeast phosphoglycerate kinase, porcine and hagfish insulin and lobster and Bacillus stearothermophilus glyceraldehyde 3-phosphate dehydrogenase. Coordinates for these proteins are held in the Protein Data Bank [151]. 

Two new immunophilins have recently been discovered which contain both FKBP and cyclophilin domains. A 37 kDa protein isolated from the Jurkat T-cell line was found to bind FK506, rapamycin, and cyclosporin A, all with high affinity.50 FKBP37 contains two FKBP domains and one cyclophilin domain, and also possesses glyceraldehyde 3-phosphate dehydrogenase activity. The 52 kDa protein, isolated from human lymphoid cells, also binds all three immunosuppressant drugs but shows no detectable rotamase activity towards a variety of peptidic substrates.95... 

Kots, A. Y., Skurai, A. V., Sergienko, E. A., Bulargina, T. V., and Sevorin, B. S. (1992). Nitroprusside stimulates the cysteine-specific mono(ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase fi"om human erythrocytes. FEES Lett. 300, 9-12. 

Goidin D, Mamessier A, Staquet MJ, Schmitt D. Berthier-Vergnes 0. Ribosomal 18S RNA prevails over glyceraldehyde-3-phosphate dehydrogenase and beta-actin genes as internal standard for quantitative comparison of mRNA levels in invasive and noninvasive human melanoma cell subpopulations. Anal Biochem 2001 295 17-21. 

Note References used are Craik et al. (1987) for rat trypsin Carter and Wells (1988) for subtilisin Nickbarg et al. (1988) for yeast trios hosphate isomerase (GAP for glyceraldehyde-3-phosphate and DHAP for dihydroxyacetone phosphate) Soukri et al. (1989) for E. coli glyceraldehyde-3-phosphate dehydrogenase Kim and Patel (1992) for human lipoamide dehydrogenase Fan et al. (1991) for yeast alcohol dehydrogenase Scrutton et al. (1990) for E. coli glutathione reductase Murphy et al. (1993) for E. coli alkaline phosphatase Leatherbarrow et al. (1985) for tyrosyl-tRNA synthetase. 

May, J. (1986). Photoaffinity Labeling of Glyceraldehyde-3-phosphate Dehydrogenase by an Aryl Azide Derivative of Glucosamine in Human Erythrocytes, J. Biol. Chem. 261 2542-2547. 

---