Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzymatic dephosphorylation of the phosphorylated forms of five different yeast enzymes has been studied: fructose-1,6-bisphosphatase, glycogen phosphorylase, neutral trehalase, NAD-glutamate dehydrogenase and 6-phosphofructo-2-kinase. Phosphorylated fructose-1,6-bisphosphatase and phosphorylated 6-phosphofructo-2-kinase were present in extracts of starved yeast cells which had been incubated for 10 min with glucose. Phosphorylated glycogen phosphorylase, neutral trehalase and NAD-glutamate dehydrogenase were obtained by incubation of yeast extract with ATP, cyclic AMP and Mg2+. After incubation with commercially available preparations of alkaline phosphatase, all five phosphorylated enzymes studied showed the changes in catalytic activity that would be expected as a consequence of dephosphorylation. The recently purified yeast enzyme which dephosphorylates phosphorylated fructose-1,6-bisophosphatase (Horn and Holzer (1987) however, was found to be active only with the phosphorylated fructose-1,6-bisphosphatase, but not with the other four phosphorylated enzymes studied. By contrast, a crude extract from yeast showed dephosphorylating activity towards all five substrates. Substrate specificity with the five phosphorylated enzymes studied of different phosphoprotein phosphatases from yeast prepared by others is discussed.
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PMID:Substrate specificity of the phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae. 284 61

The ppd1 mutant of yeast, Saccharomyces cerevisiae, was isolated as a suppressor of the cyr2 mutation which caused alteration of the catalytic subunit of cAMP-dependent protein kinase. Three peaks of phosphoprotein phosphatase activity (peak I, II and III) were identified by DEAE-Sephacel chromatography of crude extracts of the wild-type strain. The ppd1 mutant was deficient in peak III phosphoprotein phosphatase activity. The peak III enzyme efficiently utilized the phosphorylated forms of NAD-dependent glutamate dehydrogenase and trehalase as substrate. The ppd1 mutation did not suppress the cyr1, CYR3 or ras1 ras2 mutations. The ppd1 locus was located on chromosome II and had identical characteristics with glc1. The ppd1 mutation suppressed the G1 arrest caused by nutritional limitation, but maintained sensitivity to mating pheromone. In diploids homozygous for the ppd1 mutation, no premeiotic DNA replication and commitment to intragenic recombination occurred and no spores were formed, suggesting that the accumulation of phosphorylated proteins in the absence of one of the phosphoprotein phosphatases is required for mitosis but not for the initiation of meiosis.
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PMID:Isolation and characterization of a phosphoprotein phosphatase-deficient mutant in yeast. 285 99