Skip Navigation


Journal of Biochemistry Advance Access originally published online on December 6, 2008
Journal of Biochemistry 2009 145(2):249-258; doi:10.1093/jb/mvn162
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
145/2/249    most recent
mvn162v1
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 Yoshikawa, N.
Right arrow Articles by Abe, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshikawa, N.
Right arrow Articles by Abe, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Molecular Characterization of Alanine Racemase in the Kuruma Prawn Marsupenaeus japonicus{dagger}

Naoko Yoshikawa, Shigeru Okada and Hiroki Abe*

Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo, Tokyo 113-8657, Japan

*To whom correspondence should be addressed. Tel: +81-3-3301-4654, Fax: +81-3-5930-4658, E-mail: haabe{at}syd.odn.ne.jp

Received October 8, 2008; Accepted November 24, 2008


  Abstract

Aquatic crustaceans and some bivalve mollusks are known to contain copious amounts of free D-alanine in their tissues. For the first time in the animal kingdom, we have isolated a cDNA clone encoding alanine racemase from the muscle and hepatopancreas of the kuruma prawn Marsupenaeus japonicus. The recombinant enzyme expressed in Escherichia coli exhibited alanine recemase activity. The deduced amino-acid sequence showed only 23–31% identity to bacterial alanine racemases. However, the active site residues and some residues that interact with pyridoxal 5'-phosphate were also conserved in M. japonicus enzyme. There was higher alanine racemase mRNA expression in hepatopancreas than in muscle. In contrast, the D-alanine content in hepatopancreas was lower than that in muscle, suggesting that the physiological functions of free D-alanine may differ among tissues. These data suggest that the alanine racemase gene has been conserved from bacteria to invertebrates throughout a long evolutionary time scale.

Key Words: alanine racemase, aquatic invertebrate, D-alanine, D-amino acid, Marsupenaeus japonicus

Abbreviations: IPTG, isopropyl-β-D-thiogalactopyranoside; PLP, pyridoxal 5'-phosphate; RACE, rapid amplification of cDNA ends; RT, reverse transcription

{dagger}The nucleotide and deduced amino-acid sequences presented in this paper are available in the GenBank database under accession number AB097480.


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




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.