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Journal of Biochemistry Advance Access published online on January 20, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp010
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© 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 Yamauchi||, Masaru Goto§,{ddagger}, Hui-Yuan Wu||, Takuma Uo||,{Pi}, Tohru Yoshimura||,¶, Hisaaki Mihara||, Tatsuo Kurihara||, Ikuko Miyahara§, Ken Hirotsu§,* and Nobuyoshi Esaki||,*

||Institute for Chemical Research, Kyoto University
§Graduate School of Science, Osaka City University
{ddagger}Present address: Department of Biomolecular Science, Faculty of Science, Toho University, Miyama 2-2-1, Funabashi, Chiba 274-8510, Japan

*To whom correspondence should be addressed: Nobuyoshi Esaki, +81-774-38-3240, Fax: +81-774-38-3248, E-mail: esakin{at}scl.kyoto-u.ac.jp, Ken Hirotsu Tel: +81-791-58-2891, Fax: +81-791-58-2892, E-mail: hirotsu{at}spring8.or.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) 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 a-amino group of the D-alanyl moiety of the lysino-D-alanyl residue serves as a catalytic base in the same manner as the {varepsilon}-amino group of Lys57 of the original spSR.

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

{Pi}Present address: Department of Neurological Surgery, University of Washington School of Medicine, Seattle, Washington 98195-6470, USA

Present address: Department of Applied Molecular Biosciences, Graduate School of Bioagricultural


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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.
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