Intrinsic fluorescence of chloramphenicol acetyltransferase: responses to ligand binding and assignment of the contributions of tryptophan residues by site-directed mutagenesis-Reference-Cited by-同舟云学术

Intrinsic fluorescence of chloramphenicol acetyltransferase: responses to ligand binding and assignment of the contributions of tryptophan residues by site-directed mutagenesis

Published:1991-11 Issue:44 Volume:30 Page:10799-10805
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ellis Jacqueline,Murray Iain A.,Shaw William V.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00108a028

Reference23 articles.

1. Ligand interaction energies and molecular recognition by chloramphenicol acetyltransferase

2. Crystal structure of the ASP-199.fwdarw.asparagine mutant of chloramphenicol acetyltransferase to 2.35.ANG. resolution: structural consequences of disruption of a buried salt bridge

3. Analysis of the mechanism of chloramphenicol acetyltransferase by steady-state kinetics. Evidence for a ternary-complex mechanism

4. 3-(Bromoacetyl)chloramphenicol, an active site-directed inhibitor for chloramphenicol acetyltransferase

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2. Conformational Changes of the Yeast Mitochondrial Adenosine Diphosphate/Adenosine Triphosphate Carrier Studied through Its Intrinsic Fluorescence. 2. Assignment of Tryptophanyl Residues of the Carrier to the Responses to Specific Ligands;Biochemistry;1996-01-01

3. Kinetic mechanism of chloramphenicol acetyltransferase: the role of ternary complex interconversion in rate determination;Biochemistry;1995-12-01

4. Structural and Mechanistic Studies of Galactoside Acetyltransferase, the Escherichia coli LacA Gene Product;Journal of Biological Chemistry;1995-11

5. Properties of Hybrid Active Sites in Oligomeric Proteins: Kinetic and Ligand Binding Studies with Chloramphenicol Acetyltransferase Trimers;Biochemistry;1995-05-16