反硝化假单胞菌中钴胺素（I）腺苷转移酶的纯化及部分特性分析
Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans.
作者信息
Debussche L, Couder M, Thibaut D, Cameron B, Crouzet J, Blanche F
机构信息
Département Analyse, Centre de Recherche de Vitry-Alfortville, Vitry-sur-Seine, France.
出版信息
J Bacteriol. 1991 Oct;173(19):6300-2. doi: 10.1128/jb.173.19.6300-6302.1991.
Abstract
Cob(I)alamin adenosyltransferase (EC 2.5.1.17) was purified to homogeneity from extracts of a Pseudomonas denitrificans recombinant strain and sequenced at its N terminus. It is a homodimer (each unit with an Mr of 28,000) encoded by cobO. The enzyme adenosylated all of the corrinoids isolated from this microorganism but did not adenosylate cobyrinic acid.
摘要
钴胺素腺苷转移酶（EC 2.5.1.17）从反硝化假单胞菌重组菌株的提取物中纯化至同质，并对其N端进行了测序。它是由cobO编码的同型二聚体（每个亚基的Mr为28,000）。该酶能使从这种微生物中分离出的所有类咕啉腺苷化，但不能使钴胺酸腺苷化。
Zotero 插件