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Product inhibition in the radical S ‐adenosylmethionine family
Author(s) -
Challand Martin R.,
Ziegert Tillman,
Douglas Paul,
Wood Robert J.,
Kriek Marco,
Shaw Nicholas M.,
Roach Peter L.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.044
Subject(s) - chemistry , deoxyadenosine , biochemistry , methionine , tyrosine , atp synthase , stereochemistry , enzyme , amino acid
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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