Structural basis for an atypical active site of anl-aspartate/glutamate-specific racemase fromEscherichia coli-Reference-Cited by-同舟云学术

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Structural basis for an atypical active site of anl-aspartate/glutamate-specific racemase fromEscherichia coli

Published:2015-11-07 Issue:24PartB Volume:589 Page:3842-3847
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Ahn Jae-Woo,Chang Jeong Ho,Kim Kyung-Jin

Funder

National Research Foundation of Korea

MEST

Publisher

Wiley

Subject

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

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2015.11.003/fullpdf

Reference35 articles.

1. The presence of free d-serine, d-alanine and d-proline in human plasma;Nagata;Experientia,1992

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

3. Free d-serine, d-aspartate and d-alanine in central-nervous-system and serum in mutant mice lacking d-amino-acid oxidase;Hashimoto;Neurosci. Lett.,1993

4. Purification of serine racemase: biosynthesis of the neuromodulator d-serine;Wolosker;Proc. Natl. Acad. Sci. U.S.A.,1999

5. Recent advances in the formation of the bacterial peptidoglycan monomer unit;van Heijenoort;Nat. Prod. Rep.,2001

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