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学術誌査読

8 被引用数 (Scopus)


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.

ジャーナルCurrent Microbiology
出版ステータス出版済み - 4月 1 2018

!!!All Science Journal Classification (ASJC) codes

  • 微生物学
  • 応用微生物学とバイオテクノロジー


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