Modification of Residue 42 of the Active Site Loop with a Lysine-Mimetic Side Chain Rescues Isochorismate-Pyruvate Lyase Activity in Pseudomonas aeruginosa PchB-Reference-Cited by-同舟云学术

Modification of Residue 42 of the Active Site Loop with a Lysine-Mimetic Side Chain Rescues Isochorismate-Pyruvate Lyase Activity in Pseudomonas aeruginosa PchB

Published:2012-09-12 Issue:38 Volume:51 Page:7525-7532
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Olucha José¹,Meneely Kathleen M.¹,Lamb Audrey L.¹

Affiliation:

1. Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300472n

Reference52 articles.

1. Direct Brønsted Analysis of the Restoration of Activity to a Mutant Enzyme by Exogenous Amines

2. Broønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant

3. Rate-Limiting Steps and Role of Active Site Lys443 in the Mechanism of Carbapenam Synthetase

4. Chemical Rescue by Exogenous Amines of a Site-Directed Mutant of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase That Lacks a Key Lysyl Residue

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