Crystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157-Reference-Cited by-同舟云学术

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Crystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157

Published:2016-04 Issue:8 Volume:590 Page:1262-1269
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Liu Xiuhua¹,Gao Fei²,Ma Yinliang¹,Liu Shuang¹,Cui Yaqi¹,Yuan Zenglin²,Kang Xianjiang¹

Affiliation:

1. College of Life Sciences; Hebei University; Baoding China

2. State Key Laboratory of Microbial Technology; Shandong University; Jinan China

Funder

Foundation of Hebei Educational committee

Natural Science Foundation of Hebei Province

National Natural Science Funds of China

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/1873-3468.12148/fullpdf

Reference29 articles.

1. D-amino acids govern stationary phase cell wall remodeling in bacteria;Lam;Science,2009

2. Tyrocidine biosynthesis by three complementary fractions from Bacillus brevis (ATCC 8185);Roskoski;Biochemistry,1970

3. Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis;Hoffmann;J Biol Chem,1994

4. Gramicidin S-synthetase a further characterization of phenylalanine racemase, the light enzyme of gramicidin S-synthetase;Vater;Biochim Biophys Acta,1976

5. The presence of free D-serine in rat brain;Hashimoto;FEBS Lett,1992

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