Yeast glyceraldehyde-3-phosphate dehydrogenase

Kirschner, K., Eigen, M., Bittman, R. Voigt, B. (1966). The binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde 3-phosphate dehydrogenase temperature jump relaxation studies on the mechanism of an allosteric enzyme. Proceedings of the National Academy of Sciences, USA, 56, 1661-7. 

Zinc is essential for the functioning of at least twenty different enzymes, and their functions are widely varied. They include the alcohol dehydrogenases of yeast and mammalian liver, glyceraldehyde phosphate dehydrogenase, phosphoglycomutase of yeast, DNA and RNA polymerases (at least in bacteria), alkaline phosphatase in bacteria, mammalian carbo-xypeptidase, carbonic anhydrase, AMP hydrolase, pyruvate carboxylase (yeast), and aldolase (yeast and bacteria). The alkaline phosphatase of E, coli has, in each molecule, four atoms of zinc the two which maintain structure can be replaced by Mn, Co +, or Cu, whereas the other two atoms are essential for enzyme action (Trotman and Greenwood, 1971). 

Velick, S.F. (1954). The alcohol and glyceraldehyde-3-phosphate dehydrogenases of yeast and mammals. In The Mechanism of Enzyme Action. (McElroy, W.D. Glass, B., Eds.), pp. 491-519. The Johns Hopkins Press, Baltimore. 

Glyceraldehyde-3-phosphate dehydrogenase occurs widely and abundantly throughout nature. It comprises about 20% of the total soluble protein in yeast (10) and up to 10% of the soluble protein from muscle... 

L-lactate dehydrogenase and, 269 small NADH dehydrogenase and, 199 succinate dehydrogenase and, 239, 250 ubiquinone reductase and, 182, 197 yeast NADH dehydrogenase and, 219 Antiparallel sheet, glyceraldehyde-3-phosphate dehydrogenase, 13, 14 Arginine residues catalase, 395... 

Inactivation of alcohol dehydrogenase from yeast with 14C-labeled [3-(3-bromoacetylpyridinio)-propyl]-adenosine pyrophosphate followed by oxidation showed the presence of 1-carboxymethyl histidine66. After inactivation of the enzyme with labeled [3-(4-bromoacetylpyridinio)-propyl]-adenosine pyrophosphate followed by oxidation, S-carboxymethyl cysteine was identified in the protein. In the case of glyceraldehyde-3-phosphate dehydrogenase, treatment with either coenzyme analogue leads to the modification of the cysteine residue. Treatment with [14C]nicotinamide-5-bromo-4-methylimidazole dinucleotide did not reveal any modified amino-acid-residues. The labeled nicotinamide residue split off during the recovery of the inactivated enzyme. Attempts to synthesize an inactivator labeled with a 14C-acetyl residue did not give satisfactory yields. If the enzyme-coenzyme derivative was treated with tritiated sodium boron hydride, tritium could be introduced (Fig. 22). Studies with... 

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]. 

Nicotinamide-(S-methylmercury-thioinosine) dinucleotide was found to exhibit coenzyme properties with lactate dehydrogenase and liver alcohol dehydrogenase, but inactivate yeast alcohol dehydrogenase and glyceraldehyde 3-phosphate dehydrogenase an essential thiol group was therefore modified in the last two cases. 

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. 

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