Some Lactobacillus l -Lactate Dehydrogenases Exhibit Comparable Catalytic Activities for Pyruvate and Oxaloacetate-Reference-Cited by-同舟云学术

Some Lactobacillus l -Lactate Dehydrogenases Exhibit Comparable Catalytic Activities for Pyruvate and Oxaloacetate

Published:2001-01 Issue:1 Volume:183 Page:397-400
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Arai Kazuhito¹,Kamata Takeo¹,Uchikoba Hiroyuki²,Fushinobu Shinya²,Matsuzawa Hiroshi²,Taguchi Hayao¹

Affiliation:

1. Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda, Chiba 278-8510,1 and

2. Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657,2 Japan

Abstract

ABSTRACT The nonallosteric and allosteric l -lactate dehydrogenases of Lactobacillus pentosus and L. casei , respectively, exhibited broad substrate specificities, giving virtually the same maximal reaction velocity and substrate K m values for pyruvate and oxaloacetate. Replacement of Pro101 with Asn reduced the activity of the L. pentosus enzyme toward these alternative substrates to a greater extent than the activity toward pyruvate.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.183.1.397-400.2001

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