Kinetic Analysis of Pseudomonas aeruginosa Arginine Deiminase Mutants and Alternate Substrates Provides Insight into Structural Determinants of Function-Reference-Cited by-同舟云学术

Kinetic Analysis of Pseudomonas aeruginosa Arginine Deiminase Mutants and Alternate Substrates Provides Insight into Structural Determinants of Function

Published:2006-01-01 Issue:4 Volume:45 Page:1162-1172
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lu Xuefeng¹,Li Ling¹,Wu Rui¹,Feng Xiaohua¹,Li Zhimin¹,Yang Heyi¹,Wang Canhui¹,Guo Hua¹,Galkin Andrey¹,Herzberg Osnat¹,Mariano Patrick S.¹,Martin Brian M.¹,Dunaway-Mariano Debra¹

Affiliation:

1. Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131, Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, Maryland 20850, and Molecular Structure Unit, Laboratory of Neurotoxicology, NIMH, Building 10, Room 3N309, 10 Center Drive, MSC 1262, Bethesda, Maryland 20892-1262

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi051591e

Reference30 articles.

1. Crystal Structure of N-Succinylarginine Dihydrolase AstB, Bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli

2. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa

3. Structural Insight into Arginine Degradation by Arginine Deiminase, an Antibacterial and Parasite Drug Target

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