Purification and Some Properties of Citrate Synthase from Ammonia-Oxidizing Chemoautotrophic Nitrosomonas europaea ATCC 25978.
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Ammonia-oxidizing chemoautotrophic Nitrosomonas europaea ATCC 25978 exhibited remarkable oxaloacetate-oxidative activity. Citrate(si)-synthase [EC 4.1.3.7.] was purified as an electrophoretic homogeneous protein. The molecular weight of the enzyme was estimated to be about 295, 000 (αxβy) by gel filtration, suggesting that the enzyme consisted of two different subunits (α; 65, 000, β; 75, 000), as demonstrated by SDS-PAGE. The N-terminal sequences of α and β type enzyme proteins were Ala-Leu-Val-Ser-Leu-Arg-Gln-Leu-Leu. The isoelectric point of the enzyme was pH 5.2. The enzyme was stable up to 35°C and in a pH range between 6.0-8.0. The optimum pH for the reaction was 6.5-8.5 and the optimum temperature was 30-40°C. The apparent Km values for oxaloacetate and acetyl-CoA were about 0.025 and 0.080mM, respectively. The enzyme was not inhibited by ATP (1mM), NADH (1mM) or 2-oxoglutamic acid (10mM). Activation by metal ions (0.1mM) was not observed.
- 日本微生物生態学会・日本土壌微生物学会の論文
日本微生物生態学会・日本土壌微生物学会 | 論文
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