Product inhibition in the radical S-adenosylmethionine family
Product inhibition in the radical S-adenosylmethionine family
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.
iron–sulfur cluster, s-adenosylmethionine, enzyme kinetics, product inhibition
1358-1362
Challand, Martin R.
03bb1ded-9274-4525-8377-8e5930f30d65
Ziegert, Tillman
e5a19896-c311-49f4-92d0-1bbd289dd2d9
Douglas, Paul
a6304b96-3482-4468-9a45-bc05153ca270
Wood, Robert J.
f8754320-328e-4622-ac32-ef815fdae3b6
Kriek, Marco
c3e820c2-c59b-49c8-a792-f64a69e4401a
Shaw, Nicholas M.
659f54a9-df16-40f4-9d0a-115fdf91a5a1
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9
17 April 2009
Challand, Martin R.
03bb1ded-9274-4525-8377-8e5930f30d65
Ziegert, Tillman
e5a19896-c311-49f4-92d0-1bbd289dd2d9
Douglas, Paul
a6304b96-3482-4468-9a45-bc05153ca270
Wood, Robert J.
f8754320-328e-4622-ac32-ef815fdae3b6
Kriek, Marco
c3e820c2-c59b-49c8-a792-f64a69e4401a
Shaw, Nicholas M.
659f54a9-df16-40f4-9d0a-115fdf91a5a1
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9
Challand, Martin R., Ziegert, Tillman, Douglas, Paul, Wood, Robert J., Kriek, Marco, Shaw, Nicholas M. and Roach, Peter L.
(2009)
Product inhibition in the radical S-adenosylmethionine family.
FEBS Letters, 583 (8), .
(doi:10.1016/j.febslet.2009.03.044).
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.
This record has no associated files available for download.
More information
Published date: 17 April 2009
Keywords:
iron–sulfur cluster, s-adenosylmethionine, enzyme kinetics, product inhibition
Identifiers
Local EPrints ID: 146163
URI: http://eprints.soton.ac.uk/id/eprint/146163
ISSN: 0014-5793
PURE UUID: 21b6391b-f550-493d-8619-79a4c2e91520
Catalogue record
Date deposited: 21 Apr 2010 08:59
Last modified: 14 Mar 2024 00:54
Export record
Altmetrics
Contributors
Author:
Martin R. Challand
Author:
Tillman Ziegert
Author:
Paul Douglas
Author:
Robert J. Wood
Author:
Marco Kriek
Author:
Nicholas M. Shaw
Author:
Peter L. Roach
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics