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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis
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The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis

机译:嗜热古细菌激烈热球菌的氨基甲酸酯激酶样氨基甲酰磷酸合成酶,是氨基甲酰磷酸生物合成过程中缺失的环节

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摘要

Microbial carbamoyl phosphate synthetases (CPS) use glutamine as nitrogen donor and are composed of two subunits (or domains), one exhibiting glutaminase activ- ity, the other able to synthesize carbamoyl phosphate (CP) from bicarbonate, ATP, and ammonia. The pseudodimeric organization of this synthetase suggested that it has evolved by duplication of a smaller kinase, possibly a carbamate kinase (CK). In contrast to other prokaryotes the hyperthermophilic archaeon Pyrococcus furiosus was found to synthesize CP by using ammonia and not glutamine. We have purified the cognate enzyme and found it to be a dimer of two identical subunits of Mr 32,000. Its thermostability is considerable, 50/100 activity being retained after 1 h at 100 deg C or 3 h at 95 deg C.
机译:微生物氨基甲酸酯磷酸酯合成酶(CPS)使用谷氨酰胺作为氮供体,由两个亚基(或域)组成,一个具有谷氨酰胺酶活性,另一个能够从碳酸氢盐,ATP和氨中合成氨基甲酸酯磷酸酯(CP)。该合成酶的假二聚体组织表明,它是通过复制较小的激酶(可能是氨基甲酸酯激酶(CK))而进化而来的。与其他原核生物相反,发现超嗜热古生火球菌通过使用氨而不是谷氨酰胺合成CP。我们已经纯化了关联酶,发现它是Mr 32,000的两个相同亚基的二聚体。它的热稳定性非常好,在100摄氏度1小时后或在95摄氏度3小时后仍保持50/100活性。

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