Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function

Journal of Biochemistry

Volumn 119, Issue 4, 1996, Pages 703-710

  Ohmae, Eiji ^a   Iriyama, Koji ^a   Ichihara, Shigeyuki ^a   Gekko, Kunihiko ^a,b  

^a NAGOYA UNIVERSITY   (Japan)

^b HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Dihydrofolate reductase; Enzyme function; Point mutation; Role of flexible loop; Structural stability

Indexed keywords

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; GLYCINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UREA;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; POINT MUTATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

EID: 0029939820     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021299     Document Type: Article

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