Purification and some properties of IMP dehydrogenase of Bacillus cereus

Takahisa Miyamoto; Kiyoshi Matsuno; Makoto Imamura; Sam In Kim; Ken-ichi Honjoh; Shoji Hatano

doi:10.1016/S0944-5013(98)80017-7

Purification and some properties of IMP dehydrogenase of Bacillus cereus

Takahisa Miyamoto, Kiyoshi Matsuno, Makoto Imamura, Sam In Kim, Ken-ichi Honjoh, Shoji Hatano

Food Science and Biotechnology

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

4 Citations (Scopus)

Abstract

IMP dehydrogenase was purified from a crude extract of B. cereus cells. The molecular mass of the purified enzyme was estimated to be 56 kDa by SDS-PAGE and 225 kDa by gel filtration. The optimum pH of the enzyme was about 9.5. The first seven residues at N-terminus of the enzyme was determined to be Met-Trp-Glu-Ser-Lys-Phe-Val. The enzyme showed a significant specificity for inosine nucleotides among 15 purines and pyrimidines tested, but not acted on other purines and pyrimidines including inosine. Among 11 metal ions and 3 enzyme inhibitors tested, A1³⁺ activated the IMP dehydrogenase. The enzyme activity was strongly inhibited by Zn²⁺ and Fe³⁺.

Original language	English
Pages (from-to)	23-27
Number of pages	5
Journal	Microbiological Research
Volume	153
Issue number	1
DOIs	https://doi.org/10.1016/S0944-5013(98)80017-7
Publication status	Published - Jan 1 1998

All Science Journal Classification (ASJC) codes

Microbiology

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10.1016/S0944-5013(98)80017-7

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title = "Purification and some properties of IMP dehydrogenase of Bacillus cereus",

abstract = "IMP dehydrogenase was purified from a crude extract of B. cereus cells. The molecular mass of the purified enzyme was estimated to be 56 kDa by SDS-PAGE and 225 kDa by gel filtration. The optimum pH of the enzyme was about 9.5. The first seven residues at N-terminus of the enzyme was determined to be Met-Trp-Glu-Ser-Lys-Phe-Val. The enzyme showed a significant specificity for inosine nucleotides among 15 purines and pyrimidines tested, but not acted on other purines and pyrimidines including inosine. Among 11 metal ions and 3 enzyme inhibitors tested, A13+ activated the IMP dehydrogenase. The enzyme activity was strongly inhibited by Zn2+ and Fe3+.",

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T1 - Purification and some properties of IMP dehydrogenase of Bacillus cereus

AU - Miyamoto, Takahisa

AU - Matsuno, Kiyoshi

AU - Imamura, Makoto

AU - Kim, Sam In

AU - Honjoh, Ken-ichi

AU - Hatano, Shoji

PY - 1998/1/1

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N2 - IMP dehydrogenase was purified from a crude extract of B. cereus cells. The molecular mass of the purified enzyme was estimated to be 56 kDa by SDS-PAGE and 225 kDa by gel filtration. The optimum pH of the enzyme was about 9.5. The first seven residues at N-terminus of the enzyme was determined to be Met-Trp-Glu-Ser-Lys-Phe-Val. The enzyme showed a significant specificity for inosine nucleotides among 15 purines and pyrimidines tested, but not acted on other purines and pyrimidines including inosine. Among 11 metal ions and 3 enzyme inhibitors tested, A13+ activated the IMP dehydrogenase. The enzyme activity was strongly inhibited by Zn2+ and Fe3+.

AB - IMP dehydrogenase was purified from a crude extract of B. cereus cells. The molecular mass of the purified enzyme was estimated to be 56 kDa by SDS-PAGE and 225 kDa by gel filtration. The optimum pH of the enzyme was about 9.5. The first seven residues at N-terminus of the enzyme was determined to be Met-Trp-Glu-Ser-Lys-Phe-Val. The enzyme showed a significant specificity for inosine nucleotides among 15 purines and pyrimidines tested, but not acted on other purines and pyrimidines including inosine. Among 11 metal ions and 3 enzyme inhibitors tested, A13+ activated the IMP dehydrogenase. The enzyme activity was strongly inhibited by Zn2+ and Fe3+.

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