Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase

Journal of Biological Chemistry

Volumn 281, Issue 19, 2006, Pages 13234-13246

  Iwakura, Masahiro ^a   Maki, Kosuke ^a   Takahashi, Hisashi ^a   Takenawa, Tatsuyuki ^a   Yokota, Akiko ^a   Katayanagi, Katsuo ^b,c   Kamiyama, Tadashi ^b   Gekko, Kunihiko ^b  

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

^b HIROSHIMA UNIVERSITY   (Japan)

^c Structural Biology of Sakabe Project

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; CELLS; DISSOCIATION; ENZYME KINETICS; ENZYMES; RATE CONSTANTS;

DIHYDROFOLATE REDUCTASE (DHFR); DISSOCIATION CONSTANT; ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE; TERNARY COMPLEX;

ESCHERICHIA COLI;

CYSTEINE; DIHYDROFOLATE REDUCTASE; ENZYME VARIANT; METHIONINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAHYDROFOLIC ACID;

ARTICLE; BINDING KINETICS; CATALYSIS; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; R FACTOR; STEADY STATE;

BINDING SITES; CYSTEINE; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; KINETICS; METHIONINE; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; TETRAHYDROFOLATE DEHYDROGENASE;

ESCHERICHIA COLI;

EID: 33744953427     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M508823200     Document Type: Article

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