Purification and some properties of IMP dehydrogenase of Bacillus cereus.
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, Al3+ activated the IMP dehydrogenase. The enzyme activity was strongly inhibited by Zn2+ and Fe3+.
Miyamoto
T
T
Department of Food Science and Technology, Faculty of Agriculture, Kyushu University.
Matsuno
K
K
Imamura
M
M
Kim
S I
SI
Honjoh
K
K
Hatano
S
S
D000645:Ammonium Sulfate; D001409:Bacillus cereus / Q000201:enzymology* / Q000254:growth & development; D005591:Chemical Fractionation; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007168:IMP Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008670:Metals / Q000494:pharmacology; D013171:Spores, Bacterial; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D008670:Metals; D007168:IMP Dehydrogenase; D000645:Ammonium Sulfate