Transient kinetic analysis of L-serine interaction with escherichia coli D-3-phosphoglycerate dehydrogenase containing amino acid mutations in the hinge regions

Biochemistry

Volumn 50, Issue 14, 2011, Pages 2900-2906

  Grant, Gregory A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3-PHOSPHOGLYCERATE; AMINO ACID SEQUENCE; BOUND SPECIES; CONFORMATIONAL CHANGE; COOPERATIVE TRANSMISSION; COOPERATIVITY; D-3- PHOSPHOGLYCERATE DEHYDROGENASE; FLUORESCENCE QUENCHING; FREE ENZYME; HILL COEFFICIENT; KINETIC PROPERTIES; L-SERINE; MAIN EFFECT; MUTANT ENZYMES; NATIVE ENZYMES; ONE-FORM; RATE LIMITING; REGULATORY DOMAIN; SERINE BINDING; SIDE CHAINS; STEADY-STATE ANALYSIS; STRUCTURAL DOMAINS; SUBSTRATE BINDING DOMAIN; TRANSIENT KINETIC ANALYSIS;

ENZYMES; ESCHERICHIA COLI;

AMINO ACIDS;

BACTERIAL ENZYME; ESCHERICHIA COLI PHOSPHOGLYCERATE DEHYDROGENASE; GLYCINE; PHOSPHOGLYCERATE DEHYDROGENASE; SERINE; UNCLASSIFIED DRUG; VALINE;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CHEMICAL REACTION KINETICS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME MECHANISM; ESCHERICHIA COLI; FLUORESCENCE; HINGE REGION; MUTAGENESIS; MUTATIONAL ANALYSIS; NONHUMAN; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MODIFICATION; STEADY STATE;

ALGORITHMS; AMINO ACID SUBSTITUTION; AMINO ACIDS; BINDING SITES; BIOCATALYSIS; ESCHERICHIA COLI PROTEINS; GLYCINE; KINETICS; MODELS, MOLECULAR; MUTATION; PHOSPHOGLYCERATE DEHYDROGENASE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERINE; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; TIME FACTORS; VALINE;

ESCHERICHIA; ESCHERICHIA COLI;

EID: 79953724067     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200211z     Document Type: Article

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