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Journal of Bacteriology, August 2003, p. 5023-5026, Vol. 185, No. 16
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.16.5023-5026.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Conversion of Lactobacillus pentosus D-Lactate Dehydrogenase to a D-Hydroxyisocaproate Dehydrogenase through a Single Amino Acid Replacement

Chizuka Tokuda, Yoshiro Ishikura, Mayu Shigematsu, Hiroyuki Mutoh, Shino Tsuzuki, Yusaku Nakahira, Yusuke Tamura, Takeshi Shinoda, Kazuhito Arai, O Takahashi, and Hayao Taguchi*

Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, Noda, Chiba 278-8510, Japan

Received 21 March 2003/ Accepted 28 May 2003

The single amino acid replacement of Tyr52 with Leu drastically increased the activity of Lactobacillus pentosus NAD-dependent D-lactate dehydrogenase toward larger aliphatic or aromatic 2-ketoacid substrates by 3 or 4 orders of magnitude and decreased the activity toward pyruvate by about 30-fold, converting the enzyme into a highly active D-2-hydroxyisocaproate dehydrogenase.

* Corresponding author. Mailing address: Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan. Phone: 81-471-24-1501, ext. 3407. Fax: 81-471-23-9767. E-mail: htaguchi{at}rs.noda.tus.ac.jp.

Journal of Bacteriology, August 2003, p. 5023-5026, Vol. 185, No. 16
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.16.5023-5026.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J. E. T., Wouters, J. A., Yvon, M. (2009). The D-2-Hydroxyacid Dehydrogenase Incorrectly Annotated PanE Is the Sole Reduction System for Branched-Chain 2-Keto Acids in Lactococcus lactis. J. Bacteriol. 191: 873-881 [Abstract] [Full Text]  
  • Kim, J., Darley, D., Selmer, T., Buckel, W. (2006). Characterization of (R)-2-Hydroxyisocaproate Dehydrogenase and a Family III Coenzyme A Transferase Involved in Reduction of L-Leucine to Isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72: 6062-6069 [Abstract] [Full Text]  
  • Ishikura, Y., Tsuzuki, S., Takahashi, O., Tokuda, C., Nakanishi, R., Shinoda, T., Taguchi, H. (2005). Recognition Site for the Side Chain of 2-Ketoacid Substrate in D-Lactate Dehydrogenase. J Biochem 138: 741-749 [Abstract] [Full Text]  
  • Shinoda, T., Arai, K., Shigematsu-Iida, M., Ishikura, Y., Tanaka, S., Yamada, T., Kimber, M. S., Pai, E. F., Fushinobu, S., Taguchi, H. (2005). Distinct Conformation-mediated Functions of an Active Site Loop in the Catalytic Reactions of NAD-dependent D-Lactate Dehydrogenase and Formate Dehydrogenase. J. Biol. Chem. 280: 17068-17075 [Abstract] [Full Text]  


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