Subunit interactions of transcarboxylase as studied by circular dichroism.
Subunit interactions of transcarboxylase as studied by circular dichroism.
复制标题
通过圆二色性研究转羧酶的亚基相互作用。
DOI：
10.1021/bi00533a007
复制
发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
Wood,HG
中科院分区：
文献类型：
--
作者：
HennesseyJr,JP;JohnsonJr,WC;Bahler,C;Wood,HG
John P. Hennessey, Jr., W. Curtis Johnson, Jr.,* Chris Bahler, and Harland G. Wood abstract: A change in thesecondary structure of transcarboxylase resulting from quaternaryinteractions is monitored by circular dichroism spectroscopy. The change is traced to interactions among the six polypeptides that make up the 12SH subunit. It is fully reversible and is not a result of the con-ditions used to dissociate the enzyme. Our new method ofTranscarboxylase is a biotin enzyme that occurs in the propionic acid bacteria and catalyzes the transfer of a carbonyl group from methylmalonyl-CoA1 to pyruvate forming propionyl-CoA and oxaloacetate. A comprehensive review of its structure and properties has been published in 1976 (Wood & Zwolinski, 1976) and a less comprehensive review published in 1979 (Wood, 1979). A general concept of its quaternary structure has been developed by electron microscopy of the enzyme and its subunits. The central 12SH subunit appears to be cylindrical in shape and is made up of six identical
