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. 1991 Oct;173(19):6300-2.
doi: 10.1128/jb.173.19.6300-6302.1991.

Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans

L Debussche  1 , M Couder, D Thibaut, B Cameron, J Crouzet, F Blanche
Affiliations

Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans

L Debussche et al. J Bacteriol. 1991 Oct.

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.

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References

    1. J Bacteriol. 1991 Oct;173(19):6046-51 - PubMed
    1. Anal Biochem. 1990 Aug 15;189(1):24-9 - PubMed
    1. J Chromatogr. 1990 Jul 13;529(1):81-91 - PubMed
    1. J Bacteriol. 1989 Jan;171(1):547-57 - PubMed
    1. J Bacteriol. 1989 Aug;171(8):4222-31 - PubMed

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