Depletion of a highly motional residue affects formation of the Michaelis complex for Escherichia coli dihydrofolate reductase

Biochemistry

Volumn 37, Issue 18, 1998, Pages 6327-6335

  Miller, Grover Paul ^a   Benkovic, Stephen J ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; CHEMICAL MODEL; CHEMICAL STRUCTURE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; PROTEIN CONFORMATION; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 0032485627     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972922t     Document Type: Article

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