Evidence for transition-state stabilization by serine-148 in the catalytic mechanism of chloramphenicol acetyltransferase.

doi:10.1021/bi00460a016

Back to search

Article

Evidence for transition-state stabilization by serine-148 in the catalytic mechanism of chloramphenicol acetyltransferase.

Biochemistry - 27 Feb 1990

Lewendon A, Murray I A, Shaw W V, Gibbs M R, Leslie A G

Abstract excerpt

The function of conserved Ser-148 of chloramphenicol acetyltransferase (CAT) has been investigated by site-directed mutagenesis. Modeling studies (P. C. E. Moody and A. G. W. Leslie, unpublished results) suggested that the hydroxyl group of Ser-148 could be involved in transition-state stabilizat...

Topics

Acetyl Coenzyme A
Amino Acid Sequence
Catalysis
Chloramphenicol O-Acetyltransferase
Escherichia coli
Hydrolysis
Kinetics
Molecular Sequence Data
Mutation
Protein Conformation
Serine
Thermodynamics

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.