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 | |
| Publication status | Published - Jan 1 1998 |
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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 journal › Article
}
TY - JOUR
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
Y1 - 1998/1/1
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+.
UR - http://www.scopus.com/inward/record.url?scp=0032053855&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032053855&partnerID=8YFLogxK
U2 - 10.1016/S0944-5013(98)80017-7
DO - 10.1016/S0944-5013(98)80017-7
M3 - Article
C2 - 9602532
AN - SCOPUS:0032053855
VL - 153
SP - 23
EP - 27
JO - Microbiological Research
JF - Microbiological Research
SN - 0944-5013
IS - 1
ER -