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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
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/282b/208385/467af706f272/jbacter00109-0377-a.jpg

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