Purification and some properties of IMP dehydrogenase of Bacillus cereus

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

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)23-27
Number of pages5
JournalMicrobiological Research
Volume153
Issue number1
DOIs
Publication statusPublished - Jan 1 1998

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IMP Dehydrogenase
Bacillus cereus
Enzymes
Pyrimidines
Purines
Inosine Nucleotides
Inosine
Enzyme Inhibitors
Complex Mixtures
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Metals
Ions

All Science Journal Classification (ASJC) codes

  • Microbiology

Cite this

Purification and some properties of IMP dehydrogenase of Bacillus cereus. / Miyamoto, Takahisa; Matsuno, Kiyoshi; Imamura, Makoto; Kim, Sam In; Honjoh, Ken-ichi; Hatano, Shoji.

In: Microbiological Research, Vol. 153, No. 1, 01.01.1998, p. 23-27.

Research output: Contribution to journalArticle

Miyamoto, Takahisa ; Matsuno, Kiyoshi ; Imamura, Makoto ; Kim, Sam In ; Honjoh, Ken-ichi ; Hatano, Shoji. / Purification and some properties of IMP dehydrogenase of Bacillus cereus. In: Microbiological Research. 1998 ; Vol. 153, No. 1. pp. 23-27.
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