Publisher： John Wiley & Sons Inc
E-ISSN： 1521-3757|127|24|7264-7267
ISSN： 0044-8249
Source： ANGEWANDTE CHEMIE, Vol.127, Iss.24, 2015-06, pp. : 7264-7267
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Abstract
AbstractThree distinct families of ATP:corrinoid adenosyltransferases (ACATs) exist that are capable of converting vitamin B12 derivatives into coenzyme B12 by catalyzing the thermodynamically challenging reduction of CoIIrrinoids to form “supernucleophilic” CoI intermediates. While the structures and mechanisms of two of the ACAT families have been studied extensively, little is known about the EutT enzymes beyond the fact that they exhibit a unique requirement for a divalent metal cofactor for enzymatic activity. In this study we have obtained compelling evidence that EutT converts cob(II)alamin into an effectively four‐coordinate CoII species so as to facilitate CoII→CoI reduction. Intriguingly, EutT fails to promote axial ligand dissociation from the substrate analogue cob(II)inamide, a natural precursor of cob(II)alamin. This unique substrate specificity of EutT has important physiological implications.
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