Role of the S128, H186, and N187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction

Biochemistry

Volumn 45, Issue 42, 2006, Pages 12680-12686

  Li, Lei ^a,b   Zhang, Lei ^a,c   Cook, Paul F ^a  

^a UNIVERSITY OF OKLAHOMA   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^c TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; CATALYSIS; CONFORMATIONS; CRYSTAL STRUCTURE; HYDROGEN BONDS; MUTAGENESIS;

6-PHOSPHOGLUCONATE DEHYDROGENASE (6PGDH); DECARBOXYLATION; MUTANT ENZYMES; MUTATION;

ENZYME KINETICS;

3 KETO 6 PHOSPHOGLUCONATE; CARBON 13; DEUTERIUM; OXIDOREDUCTASE; PHOSPHOGLUCONATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DECARBOXYLATION; ENZYME ASSAY; ENZYME BINDING; HYDROGEN BOND; ISOTOPE LABELING; LIVER; NONHUMAN; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; SHEEP; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; DNA PRIMERS; KINETICS; LIVER; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHOGLUCONATE DEHYDROGENASE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SHEEP;

OVIS ARIES;

EID: 33750330975     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0613675     Document Type: Article

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