Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv-Reference-Cited by-同舟云学术

Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv

Published:2015-02-01 Issue:2 Volume:79 Page:236-238
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Mori Shigetarou¹,Kim Hyun¹,Rimbara Emiko¹,Arakawa Yoshichika²,Shibayama Keigo¹

Affiliation:

1. Department of Bacteriology II, National Institute of Infectious Diseases, Musashi-Murayama, Japan

2. Department of Bacteriology, Nagoya University Graduate School of Medicine, Nagoya, Japan

Abstract

Abstract Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A) phosphorylase from Mycobacterium tuberculosis H37Rv (MtAPA) belongs to the histidine triad motif (HIT) superfamily, but is the only member with an alanine residue at position 149 (Ala-149). Enzymatic analysis revealed that the Ala-149 deletion mutant displayed substrate specificity for diadenosine 5′,5′′′-P1,P5-pentaphosphate and was inactive on Ap4A and other substrates that are utilized by the wild-type enzyme.

Funder

Ministry of Health, Labor, and Welfare of Japan

Young Scientists (B) from the Ministry of Education, Culture, Sports, Science and Technology of Japan

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/79/2/236/36807783/bbb0236.pdf

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