Catalytic Activity Profile of Polyphosphate Kinase 1 from Myxococcus xanthus

Shiori Kamatani, Kaoru Takegawa, Yoshio Kimura

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

Polyphosphate kinase 1 (Ppk1) catalyzes reverse transfer of the terminal phosphate from ATP to form polyphosphate (polyP) and from polyP to form ATP, and is responsible for the synthesis of most of cellular polyPs. When Ppk1 from Myxococcus xanthus was incubated with 0.2 mM polyP60−70 and 1 mM ATP or ADP, the rate of ATP synthesis was approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeded one-third, the equilibrium shifted to ATP synthesis, suggesting that M. xanthus Ppk1 preferentially catalyzed ATP formation. At the same time, GTP and GDP were not recognized as substrates by Ppk1. In the absence of polyP, Ppk1 generated ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzed the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity.

元の言語英語
ページ(範囲)379-385
ページ数7
ジャーナルCurrent Microbiology
75
発行部数4
DOI
出版物ステータス出版済み - 4 1 2018

Fingerprint

Myxococcus xanthus
Adenosine Triphosphate
Adenosine Diphosphate
Polyphosphates
Adenosine Monophosphate
Phosphates
polyphosphate kinase
Adenylate Kinase
Polyps
Guanosine Triphosphate

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology

これを引用

Catalytic Activity Profile of Polyphosphate Kinase 1 from Myxococcus xanthus. / Kamatani, Shiori; Takegawa, Kaoru; Kimura, Yoshio.

:: Current Microbiology, 巻 75, 番号 4, 01.04.2018, p. 379-385.

研究成果: ジャーナルへの寄稿記事

Kamatani, Shiori ; Takegawa, Kaoru ; Kimura, Yoshio. / Catalytic Activity Profile of Polyphosphate Kinase 1 from Myxococcus xanthus. :: Current Microbiology. 2018 ; 巻 75, 番号 4. pp. 379-385.
@article{9a26697b8c944ad1bc57295e049a21e4,
title = "Catalytic Activity Profile of Polyphosphate Kinase 1 from Myxococcus xanthus",
abstract = "Polyphosphate kinase 1 (Ppk1) catalyzes reverse transfer of the terminal phosphate from ATP to form polyphosphate (polyP) and from polyP to form ATP, and is responsible for the synthesis of most of cellular polyPs. When Ppk1 from Myxococcus xanthus was incubated with 0.2 mM polyP60−70 and 1 mM ATP or ADP, the rate of ATP synthesis was approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeded one-third, the equilibrium shifted to ATP synthesis, suggesting that M. xanthus Ppk1 preferentially catalyzed ATP formation. At the same time, GTP and GDP were not recognized as substrates by Ppk1. In the absence of polyP, Ppk1 generated ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzed the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity.",
author = "Shiori Kamatani and Kaoru Takegawa and Yoshio Kimura",
year = "2018",
month = "4",
day = "1",
doi = "10.1007/s00284-017-1391-y",
language = "English",
volume = "75",
pages = "379--385",
journal = "Current Microbiology",
issn = "0343-8651",
publisher = "Springer New York",
number = "4",

}

TY - JOUR

T1 - Catalytic Activity Profile of Polyphosphate Kinase 1 from Myxococcus xanthus

AU - Kamatani, Shiori

AU - Takegawa, Kaoru

AU - Kimura, Yoshio

PY - 2018/4/1

Y1 - 2018/4/1

N2 - Polyphosphate kinase 1 (Ppk1) catalyzes reverse transfer of the terminal phosphate from ATP to form polyphosphate (polyP) and from polyP to form ATP, and is responsible for the synthesis of most of cellular polyPs. When Ppk1 from Myxococcus xanthus was incubated with 0.2 mM polyP60−70 and 1 mM ATP or ADP, the rate of ATP synthesis was approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeded one-third, the equilibrium shifted to ATP synthesis, suggesting that M. xanthus Ppk1 preferentially catalyzed ATP formation. At the same time, GTP and GDP were not recognized as substrates by Ppk1. In the absence of polyP, Ppk1 generated ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzed the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity.

AB - Polyphosphate kinase 1 (Ppk1) catalyzes reverse transfer of the terminal phosphate from ATP to form polyphosphate (polyP) and from polyP to form ATP, and is responsible for the synthesis of most of cellular polyPs. When Ppk1 from Myxococcus xanthus was incubated with 0.2 mM polyP60−70 and 1 mM ATP or ADP, the rate of ATP synthesis was approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeded one-third, the equilibrium shifted to ATP synthesis, suggesting that M. xanthus Ppk1 preferentially catalyzed ATP formation. At the same time, GTP and GDP were not recognized as substrates by Ppk1. In the absence of polyP, Ppk1 generated ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzed the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity.

UR - http://www.scopus.com/inward/record.url?scp=85033461432&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85033461432&partnerID=8YFLogxK

U2 - 10.1007/s00284-017-1391-y

DO - 10.1007/s00284-017-1391-y

M3 - Article

VL - 75

SP - 379

EP - 385

JO - Current Microbiology

JF - Current Microbiology

SN - 0343-8651

IS - 4

ER -