Monomeric Corynebacterium glutamicum N-acetyl glutamate kinase maintains sensitivity to L-arginine but has a lower intrinsic catalytic activity-Reference-Cited by-同舟云学术

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Monomeric Corynebacterium glutamicum N-acetyl glutamate kinase maintains sensitivity to L-arginine but has a lower intrinsic catalytic activity

Published:2015-10-29 Issue:4 Volume:100 Page:1789-1798
ISSN:0175-7598
Container-title:Applied Microbiology and Biotechnology
language:en
Short-container-title:Appl Microbiol Biotechnol

Author:

Huang Yuanyuan,Li Cheng,Zhang Hao,Liang Shuli,Han Shuangyan,Lin Ying,Yang Xiaorong,Zheng Suiping

Funder

National Natural Science Foundation of China

National Key Technology Support Program

Chinese Academy of Sciences

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s00253-015-7065-4.pdf

Reference17 articles.

1. Cunin R, Glansdorff N, Pierard A, Stalon V (1986) Biosynthesis and metabolism of arginine in bacteria. Microbiol Rev 50(3):314

2. Fernández-Murga ML, Rubio V (2008) Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes. J Bacteriol 190(8):3018–3025. doi: 10.1128/JB.01831-07

3. Fernández-Murga ML, Gil-Ortiz F, Llácer JL, Rubio V (2004) Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase. J Bacteriol 186(18):6142–6149. doi: 10.1128/JB.186.18.6142-6149.2004

4. Gil-Ortiz F, Ramón-Maiques S, Fernández-Murga ML, Fita I, Rubio V (2010) Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations. J Mol Biol 399(3):476–490. doi: 10.1016/j.jmb.2010.04.025

5. Haas D, Leisinger T (1975) N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Catalytic and regulatory properties. Eur J Biochem/FEBS 52(2):377–393. doi: 10.1111/j.1432-1033.1975.tb04005.x

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