HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 7, 5329-5335, February 18, 2005

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 280/7/5329    most recent M411918200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Muramatsu, H. Articles by Esaki, N. Search for Related Content PubMed PubMed Citation Articles by Muramatsu, H. Articles by Esaki, N. Social Bookmarking                      What's this?

The Putative Malate/Lactate Dehydrogenase from Pseudomonas putida Is an NADPH-dependent ¹-Piperideine-2-carboxylate/¹-Pyrroline-2-carboxylate Reductase Involved in the Catabolism of D-Lysine and D-Proline^*

Hisashi Muramatsu, Hisaaki Mihara, Ryo Kakutani, Mari Yasuda¶, Makoto Ueda¶, Tatsuo Kurihara, and Nobuyoshi Esaki||

From the Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan and the ^¶Yokohama Research Center, Mitsubishi Chemical Corporation, Yokohama 227-8502, Japan

A Pseudomonas putida ATCC12633 gene, dpkA, encoding a putative protein annotated as malate/L-lactate dehydrogenase in various sequence data bases was disrupted by homologous recombination. The resultant dpkA^– mutant was deprived of the ability to use D-lysine and also D-proline as a sole carbon source. The dpkA gene was cloned and overexpressed in Escherichia coli, and the gene product was characterized. The enzyme showed neither malate dehydrogenase nor lactate dehydrogenase activity but catalyzed the NADPH-dependent reduction of such cyclic imines as ¹-piperideine-2-carboxylate and ¹-pyrroline-2-carboxylate to form L-pipecolate and L-proline, respectively. NADH also served as a hydrogen donor for both substrates, although the reaction rates were less than 1% of those with NADPH. The reverse reactions were also catalyzed by the enzyme but at much lower rates. Thus, the enzyme has dual metabolic functions, and we named the enzyme ¹-piperideine-2-carboxylate/¹-pyrroline-2-carboxylate reductase, the first member of a novel subclass in a large family of NAD(P)-dependent oxidoreductases.

Received for publication, October 20, 2004 , and in revised form, November 22, 2004.

^* This work was supported in part by Grant-in-aid for Scientific Research on Priority Areas (B) 13125203 (to N. E.) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan, by Grant-in-aid for Encouragement of Young Scientists 15780070 (to H. Mihara) from the Japan Society for the Promotion of Science, by the National Project on Protein Structural and Functional Analyses, and by a grant-in-aid from the Ministry of Education, Culture, Sports, Science, and Technology, Japan (21st Century COE on Kyoto University Alliance for Chemistry). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

These authors contributed equally to this work.

^|| To whom correspondence should be addressed. Tel.: 81-774-38-3240; Fax: 81-774-38-3248; E-mail: esaki{at}scl.kyoto-u.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. R. Hristova, R. Schmidt, A. Y. Chakicherla, T. C. Legler, J. Wu, P. S. Chain, K. M. Scow, and S. R. Kane Comparative Transcriptome Analysis of Methylibium petroleiphilum PM1 Exposed to the Fuel Oxygenates Methyl tert-Butyl Ether and Ethanol Appl. Envir. Microbiol., November 15, 2007; 73(22): 7347 - 7357. [Abstract] [Full Text] [PDF]

				O. Revelles, R.-M. Wittich, and J. L. Ramos Identification of the Initial Steps in D-Lysine Catabolism in Pseudomonas putida J. Bacteriol., April 1, 2007; 189(7): 2787 - 2792. [Abstract] [Full Text] [PDF]

				M. Goto, H. Muramatsu, H. Mihara, T. Kurihara, N. Esaki, R. Omi, I. Miyahara, and K. Hirotsu Crystal Structures of {Delta}1-Piperideine-2-carboxylate/{Delta}1-Pyrroline-2-carboxylate Reductase Belonging to a New Family of NAD(P)H-dependent Oxidoreductases: CONFORMATIONAL CHANGE, SUBSTRATE RECOGNITION, AND STEREOCHEMISTRY OF THE REACTION J. Biol. Chem., December 9, 2005; 280(49): 40875 - 40884. [Abstract] [Full Text] [PDF]

				O. Revelles, M. Espinosa-Urgel, T. Fuhrer, U. Sauer, and J. L. Ramos Multiple and Interconnected Pathways for L-Lysine Catabolism in Pseudomonas putida KT2440 J. Bacteriol., November 1, 2005; 187(21): 7500 - 7510. [Abstract] [Full Text] [PDF]