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- Title
Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co<sup>I</sup>rrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co<sup>II</sup>rrinoids.
- Authors
Park, Kiyoung; Mera, Paola E.; Moore, Theodore C.; Escalante-Semerena, Jorge C.; Brunold, Thomas C.
- Abstract
Three 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.
- Subjects
SALMONELLA enterica; CORRINOIDS; ADENOSINE triphosphate; COFACTORS (Biochemistry); ETHANOLAMINES; RIBONUCLEOTIDES
- Publication
Angewandte Chemie International Edition, 2015, Vol 54, Issue 24, p7158
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201501930