Product inhibition in the radical S-adenosylmethionine family - PubMed (original) (raw)
. 2009 Apr 17;583(8):1358-62.
doi: 10.1016/j.febslet.2009.03.044. Epub 2009 Mar 26.
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- PMID: 19328201
- DOI: 10.1016/j.febslet.2009.03.044
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Product inhibition in the radical S-adenosylmethionine family
Martin R Challand et al. FEBS Lett. 2009.
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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.
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