The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity
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Modification of pig M4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residuePyridine analogs inhibit the glucosyltransferase of Streptococcus mutans.Equilibrium protection studies of the interaction of bovine glutamate dehydrogenase with purine nucleotide effectors.Affinity labelling of the NADP+-binding site of glucose 6-phosphate dehydrogenase from Candida utilis.Ox liver glutamate dehydrogenase. The role of lysine-126 reappraised in the light of studies of inhibition and inactivation by pyridoxal 5'-phosphate.Horse liver alcohol dehydrogenase. A study of the essential lysine residue.Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5'-phosphate.Dogfish M4 lactate dehydrogenase: reversible inactivation by pyridoxal 5'-phosphate and complete protection in complexes that mimic the active ternary complex.Calf-spleen nicotinamide-adenine dinucleotide glycohydrolase. Properties of the active site.The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.Is pyridoxal 5'-phosphate an affinity label for phosphate-binding sites in proteins?: The case of bovine glutamate dehydrogenase.Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds.The use of pH-gradient ion-exchange chromatography to separate sheep liver cytoplasmic aldehyde dehydrogenase from mitochondrial enzyme contamination, and observations on the interaction between the pure cytoplasmic enzyme and disulfiramThe purification and some properties of the Mg(2+)-activated cytosolic aldehyde dehydrogenase of Saccharomyces cerevisiae.Inactivation of penicillin acylase from Kluyvera citrophila by N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline: a case of time-dependent non-covalent enzyme inhibition.Kinetic analysis of regeneration by dilution of a covalently modified protein.Kinetic analysis of protein modification reactions at equilibriumModification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residueSuccinylation and inactivation of 3-hydroxy-3-methylglutaryl-CoA synthase by succinyl-CoA and its possible relevance to the control of ketogenesis.Modification of mouse testicular lactate dehydrogenase by pyridoxal 5'-phosphate.Cassette mutagenesis of lysine 130 of human glutamate dehydrogenase. An essential residue in catalysis.Essential arginine residues in glutamate dehydrogenase.The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.Subunit assembly and active site location in the structure of glutamate dehydrogenase.ESR investigations of free and immobilized glutamate dehydrogenase.Inactivation of enoyl-CoA reductase in pigeon liver fatty acid synthetase by pyridoxal 5'-phosphate: evidence for the presence of one lysine residue at the active site.
P2860
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P2860
The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity
description
1975 nî lūn-bûn
@nan
1975年の論文
@ja
1975年論文
@yue
1975年論文
@zh-hant
1975年論文
@zh-hk
1975年論文
@zh-mo
1975年論文
@zh-tw
1975年论文
@wuu
1975年论文
@zh
1975年论文
@zh-cn
name
The equilibrium position of th ...... y abolishes catalytic activity
@en
type
label
The equilibrium position of th ...... y abolishes catalytic activity
@en
prefLabel
The equilibrium position of th ...... y abolishes catalytic activity
@en
P2860
P356
P1433
P1476
The equilibrium position of th ...... y abolishes catalytic activity
@en
P2093
P2860
P304
P356
10.1042/BJ1470351
P407
P577
1975-05-01T00:00:00Z