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

Shigetarou Mori; Hyun Kim; Emiko Rimbara; Yoshichika Arakawa; Keigo Shibayama

doi:10.1080/09168451.2014.973364

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

Shigetarou Mori
, Hyun Kim
, Emiko Rimbara
, Yoshichika Arakawa
, Keigo Shibayama

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	236-238
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	79
Issue number	2
DOIs	https://doi.org/10.1080/09168451.2014.973364
Publication status	Published - 2015
Externally published	Yes

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This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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10.1080/09168451.2014.973364

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

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.",

keywords = "Drug target, Kinetics, Mycobacteria, Phosphorylase",

author = "Shigetarou Mori and Hyun Kim and Emiko Rimbara and Yoshichika Arakawa and Keigo Shibayama",

note = "Publisher Copyright: {\textcopyright} 2014 Japan Society for Bioscience, Biotechnology, and Agrochemistry.",

year = "2015",

doi = "10.1080/09168451.2014.973364",

language = "English",

volume = "79",

pages = "236--238",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Oxford University Press",

number = "2",

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TY - JOUR

T1 - Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv

AU - Mori, Shigetarou

AU - Kim, Hyun

AU - Rimbara, Emiko

AU - Arakawa, Yoshichika

AU - Shibayama, Keigo

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - Drug target

KW - Kinetics

KW - Mycobacteria

KW - Phosphorylase

UR - https://www.scopus.com/pages/publications/84928890255

UR - https://www.scopus.com/pages/publications/84928890255#tab=citedBy

U2 - 10.1080/09168451.2014.973364

DO - 10.1080/09168451.2014.973364

M3 - Article

C2 - 25348769

AN - SCOPUS:84928890255

SN - 0916-8451

VL - 79

SP - 236

EP - 238

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 2

ER -

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

Abstract

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