Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans.
نویسندگان
چکیده
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.
منابع مشابه
Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica.
ATP:cob(I)alamin adenosyltransferase (EutT) of Salmonella enterica was overproduced and enriched to approximately 70% homogeneity, and its basic kinetic parameters were determined. Abundant amounts of EutT protein were produced, but all of it remained insoluble. Soluble active EutT protein (approximately 70% homogeneous) was obtained after treatment with detergent. Under conditions in which cob...
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متن کاملPurification and Initial Biochemical Characterization of the ATP:Cob(I)alamin Adenosyltransferase(EutT) Enzyme of Salmonella enterica
The ATP:Co(I)balamin adenosyltransferase (EutT) enzyme of Salmonella enterica was overproduced, enriched to ~70% homogeneity, and its basic kinetic parameters were determined. Abundant amounts of EutT protein were produced, but all of it remained insoluble. Soluble, active EutT protein (~70% homogeneous) was obtained after treatment with detergent. Under conditions where Cbl was saturating, the...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 173 19 شماره
صفحات -
تاریخ انتشار 1991