Abstract
The first step in the biosynthesis of the molybdopterin cofactor involves an unprecedented insertion of the purine C8 carbon between the C2' and C3' carbons of the ribose moiety of GTP. Here we review mechanistic studies on this remarkable transformation. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications.
Keywords:
Intermediate trapping; Mechanism; MoaA; Molybtopterin; Substrate analog.
Copyright © 2015 Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Biocatalysis*
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Carbon
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Coenzymes / biosynthesis*
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Escherichia coli Proteins / physiology*
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Guanosine Triphosphate / chemistry*
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Humans
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Isomerases / physiology*
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Metalloproteins / biosynthesis*
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Molybdenum Cofactors
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Pteridines
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Purines / chemistry*
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Ribose / chemistry*
Substances
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Coenzymes
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Escherichia coli Proteins
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Metalloproteins
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Molybdenum Cofactors
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Pteridines
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Purines
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Ribose
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Carbon
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Guanosine Triphosphate
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molybdenum cofactor
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Isomerases
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MoaA protein, E coli
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purine