Skip Navigation


Journal of Biochemistry Advance Access originally published online on January 20, 2009
Journal of Biochemistry 2009 145(4):421-424; doi:10.1093/jb/mvp010
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
145/4/421    most recent
mvp010v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Yamauchi, T.
Right arrow Articles by Esaki, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamauchi, T.
Right arrow Articles by Esaki, N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Rapid Communication

Serine Racemase with Catalytically Active Lysinoalanyl Residue*

Takae Yamauchi1, Masaru Goto2,{dagger}, Hui-Yuan Wu1, Takuma Uo1,{dagger}, Tohru Yoshimura1,{dagger}, Hisaaki Mihara1, Tatsuo Kurihara1, Ikuko Miyahara2, Ken Hirotsu2,{ddagger} and Nobuyoshi Esaki1,§

1Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011; and 2Graduate School of Science, Osaka City University, Osaka 558-8585, Japan

§To whom correspondence should be addressed. Tel: +81 774 38 3240, Fax: +81 774 38 3248, E-mail: esakin{at}scl.kyoto-u.ac.jp

Received December 19, 2008; Accepted January 10, 2009


  Abstract

Serine racemase synthesizes D-serine, a physiological agonist of the NMDA receptor in mammalian brains. Schizosaccharomyces pombe produces serine racemase (spSR) that is highly similar to the brain enzyme. Our mass-spectrometric and X-ray studies revealed that spSR is modified with its natural substrate serine. spSR remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-L-lysyl (lysino-D-alanyl) residue. This indicates that the {alpha}-amino group of the D-alanyl moiety of the lysino-D-alanyl residue serves as a catalytic base in the same manner as the {epsilon}-amino group of Lys57 of the original spSR.

Key Words: D-serine, modification, pyridoxal 5'-phosphate, racemase, Schizosaccharomyces pombe

Abbreviations: ATP, adenosine triphosphate; ESI, electrospray ionization; NMDA, N-methyl-D-aspartate; NMR, nuclear magnetic resonance; PCR, polymerase chain reaction; PLP, pyridoxal 5'-phosphate

{ddagger}Correspondence may also be addressed. Tel: +81 791 58 2891, Fax: +81 791 58 2892, E-mail: hirotsu{at}spring8.or.jp

{dagger}Present address: Masaru Goto, Department of Biomolecular Science, Faculty of Science, Toho University, Miyama 2-2-1, Funabashi, Chiba 274-8510, Japan; Takuma Uo, Department of Neurological Surgery, University of Washington School of Medicine, Seattle, Washington 98195-6470, USA; Tohru Yoshimura, Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Aichi, Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. Goto, T. Yamauchi, N. Kamiya, I. Miyahara, T. Yoshimura, H. Mihara, T. Kurihara, K. Hirotsu, and N. Esaki
Crystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombe
J. Biol. Chem., September 18, 2009; 284(38): 25944 - 25952.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.