Biochemical Characteristics of Microcystin LR Degradation by Typical Protease

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  • OKANO KUNIHIRO
    Graduate School of Life and Environmental Sciences, University of Tsukuba
  • MASEDA HIDEAKI
    Graduate School of Life and Environmental Sciences, University of Tsukuba
  • SUGITA KAZUTOSHI
    Dia Analysis Service Inc./8-5-1 Tyuuou, Ami, Inashiki 300-0332, Japan
  • SAITO TAKESHI
    Safety and Microbial Control Research Center, Kao Corporation
  • UTSUMI MOTOO
    Graduate School of Life and Environmental Sciences, University of Tsukuba
  • MAEKAWA TAKAAKI
    Graduate School of Life and Environmental Sciences, University of Tsukuba
  • KOBAYASHI MICHIHIKO
    Graduate School of Life and Environmental Sciences, University of Tsukuba
  • SUGIURA NORIO
    Graduate School of Life and Environmental Sciences, University of Tsukuba

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Other Title
  • 代表的なプロテアーゼによるmicrocystin LR分解の生化学的特性

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Abstract

In this study, effect of pH value on the stability of microcystin LR, potential of the degradation by typical proteases and its initial degradation process by cell free extract (CE) of Novosphingobium (synonym: Sphingomonas) sp. MD-1 using mass spectrometry (MS) were examined in vitro studies. Microcystin LR was stable within a wide range of pH 2-11. Cyclic microcystin LR was also stable to 12 kinds of proteases, and was not degraded at all. MlrA (microcystinase) and its homologous enzymes were found to be very specific enzymes. Initial linearized microcystin LR by the CE of microcystin-degrading bacteria Novosphingobium sp. MD-1 was identified by MS. The linearized microcystin LR was found to be the same structure as the intermediate by Novosphingobium (synonym: Sphingomonas) sp. ACM3962 and Sphingomonas sp. B91–2). The identified linearized microcystin LR was degraded by 9 kinds of proteases, and the cleavage was considered to start from L-Arg in the C-terminal. However, those activities were extremely low compared with CE of Novoshpingobium sp. MD-1. Therefore, mlrA gene cluster including MlrA and MlrB was found to be a highly specific and rare enzyme group in the microcystin LR degradation.

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