Kinetic studies of protein farnesyltransferase mutants establish active substrate conformation

Biochemistry

Volumn 42, Issue 32, 2003, Pages 9741-9748

  Pickett, Jennifer S ^a   Bowers, Katherine E ^a   Hartman, Heather L ^a   Fu, Hua Wen ^b,c   Embry, Alan C ^b   Casey, Patrick J ^b   Fierke, Carol A ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; CRYSTAL STRUCTURE; ENZYMES; GROUND STATE; HYDROGEN BONDS; METALLORGANIC POLYMERS; RATE CONSTANTS;

MUTANTS;

BIOCHEMISTRY;

FARNESYL DIPHOSPHATE; PROTEIN FARNESYLTRANSFERASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL;

ALKYL AND ARYL TRANSFERASES; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; FARNESYLTRANSTRANSFERASE; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MAGNESIUM; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POLYISOPRENYL PHOSPHATES; PROTEIN CONFORMATION; PROTEIN ISOPRENYLATION; RATS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TRITIUM;

EID: 0043028384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0346852     Document Type: Article

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