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乙酸激酶和磷酸转乙酰酶。

Acetate kinase and phosphotransacetylase.

作者信息

Ferry James G

机构信息

Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania, USA.

出版信息

Methods Enzymol. 2011;494:219-31. doi: 10.1016/B978-0-12-385112-3.00011-1.

Abstract

Most of the methane produced in nature derives from the methyl group of acetate, the major end product of anaerobes decomposing complex plant material. The acetate is derived from the metabolic intermediate acetyl-CoA via the combined activities of phosphotransacetylase and acetate kinase. In Methanosarcina species, the enzymes function in the reverse direction to activate acetate to acetyl-CoA prior to cleavage into a methyl and carbonyl group of which the latter is oxidized providing electrons for reduction of the former to methane. Thus, phosphotransacetylase and acetate kinase have a central role in the conversion of complex organic matter to methane by anaerobic microbial food chains. Both enzymes have been purified from Methanosarcina thermophila and characterized. Both enzymes from M. thermophila have also been produced in Escherichia coli permitting crystal structures and amino acid variants, the kinetic and biochemical studies of which have lead to proposals for catalytic mechanisms. The high identity of both enzymes to paralogs in the domain Bacteria suggests ancient origins and common mechanisms.

摘要

自然界中产生的大部分甲烷来源于乙酸的甲基,乙酸是厌氧菌分解复杂植物物质的主要终产物。乙酸通过磷酸转乙酰酶和乙酸激酶的联合作用,从代谢中间体乙酰辅酶A衍生而来。在甲烷八叠球菌属中,这些酶以相反的方向发挥作用,在乙酸裂解为一个甲基和一个羰基之前,将乙酸激活为乙酰辅酶A,其中后者被氧化,为前者还原为甲烷提供电子。因此,磷酸转乙酰酶和乙酸激酶在厌氧微生物食物链将复杂有机物转化为甲烷的过程中起着核心作用。这两种酶都已从嗜热甲烷八叠球菌中纯化并进行了表征。嗜热甲烷八叠球菌的这两种酶也已在大肠杆菌中产生,从而获得了晶体结构和氨基酸变体,对其进行的动力学和生化研究提出了催化机制。这两种酶与细菌域中的旁系同源物具有高度的同一性,表明它们起源古老且机制相同。

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