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- Title
Product inhibition in the radical S-adenosylmethionine family
- Authors
Challand, Martin R.; Ziegert, Tillman; Douglas, Paul; Wood, Robert J.; Kriek, Marco; Shaw, Nicholas M.; Roach, Peter L.
- Abstract
Abstract: Members of the radical S-adenosylmethionine (AdoMet) superfamily reductively cleave AdoMet to generate the highly reactive 5′-deoxyadenosyl radical (DOA) which initiates biological transformations by abstraction of a hydrogen atom. We demonstrate that three members of the family: biotin synthase (BioB), lipoyl synthase (LipA) and tyrosine lyase (ThiH) are inhibited in vitro by a combination of the products 5′-deoxyadenosine (DOA) and methionine. These results suggest the observed inhibition is a common feature of the radical AdoMet proteins that form DOA and methionine as products. Addition of 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) to BioB, LipA or ThiH activity assays removed the product inhibition by catalysing the hydrolysis of DOA and gave an increase in activity.
- Subjects
ENZYME inhibitors; ADENOSYLMETHIONINE; RADICALS (Chemistry); BIOTRANSFORMATION (Metabolism); HOMOCYSTEINE; LYASES; NUCLEOSIDASES; METHYLTHIOADENOSINE
- Publication
FEBS Letters, 2009, Vol 583, Issue 8, p1358
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.03.044