Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase

Biochemistry

Volumn 48, Issue 22, 2009, Pages 4808-4815

  Burton, Rodney L ^a,b   Chen, Shawei ^a   Xiao, Lan Xu ^a   Grant, Gregory A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALLOSTERIC SITE; ANION-BINDING; D-3- PHOSPHOGLYCERATE DEHYDROGENASE; FLUORESCENCE RESONANCE ENERGY TRANSFER ANALYSIS; L-SERINE; LOW LEVEL; MYCOBACTERIUM TUBERCULOSIS; NADH OXIDATION; PHENYLALANINE RESIDUES; PHYSIOLOGICAL SUBSTRATE; POTENTIAL MECHANISM; REGULATORY DOMAIN; STEADY STATE; SUBSTRATE CONCENTRATIONS; SUBSTRATE INHIBITION; TRANSIENT KINETIC DATA; TRYPTOPHAN RESIDUES;

AMINO ACIDS; BINDING ENERGY; ENERGY TRANSFER; ENZYMES; FLUORESCENCE; LAWS AND LEGISLATION; NEGATIVE IONS; PLANTS (BOTANY); SUBSTRATES;

BINDING SITES;

PHOSPHOGLYCERATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BINDING SITE; CATALYSIS; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE RESONANCE ENERGY TRANSFER; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; SIMULATION;

ALLOSTERIC SITE; AMINO ACID SUBSTITUTION; ANIONS; BINDING, COMPETITIVE; CATALYSIS; KINETICS; MYCOBACTERIUM TUBERCULOSIS; NAD; PHOSPHOGLYCERATE DEHYDROGENASE; PROTEIN STRUCTURE, TERTIARY; SERINE; SUBSTRATE SPECIFICITY;

MYCOBACTERIUM TUBERCULOSIS;

EID: 66649133096     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900172q     Document Type: Article

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