Probing the roles of conserved arginine-44 of Escherichia coli dihydrofolate reductase in its function and stability by systematic sequence perturbation analysis

Biochemical and Biophysical Research Communications

Volumn 391, Issue 4, 2010, Pages 1703-1707

  Yokota, Akiko ^a   Takahashi, Hisashi ^a   Takenawa, Tatsuyuki ^a   Arai, Munehito ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Amino acid indices; Catalytic activity; Dihydrofolate reductase; Sequence perturbation analysis; Stability; Systematic amino acid substitutions

Indexed keywords

ARGININE; DIHYDROFOLATE REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ELECTRIC ACTIVITY; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROPHOBICITY; MOLECULAR PROBE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FUNCTION; PROTEIN STABILITY; RNA TRANSLATION; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARGININE; CONSERVED SEQUENCE; ENZYME STABILITY; ESCHERICHIA COLI; MUTATION; NADP; PROTEIN CONFORMATION; TETRAHYDROFOLATE DEHYDROGENASE;

ESCHERICHIA COLI;

EID: 74449091577     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.12.134     Document Type: Article

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