Abstract
The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.
Keywords:
(de)Carboxylase; Cycloaddition; Prenyl transferase; Prenylated FMN; UbiD; UbiX.
Copyright © 2017 Elsevier Inc. All rights reserved.
MeSH terms
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Carboxy-Lyases* / chemistry
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Carboxy-Lyases* / genetics
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Carboxy-Lyases* / metabolism
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Dimethylallyltranstransferase* / chemistry
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Dimethylallyltranstransferase* / genetics
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Dimethylallyltranstransferase* / metabolism
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Escherichia coli Proteins* / chemistry
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Escherichia coli Proteins* / genetics
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Escherichia coli Proteins* / metabolism
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Escherichia coli* / chemistry
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Escherichia coli* / genetics
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Escherichia coli* / metabolism
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Flavins* / biosynthesis
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Flavins* / chemistry
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Flavins* / genetics
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Flavoproteins* / chemistry
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Flavoproteins* / genetics
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Flavoproteins* / metabolism
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Prenylation / physiology*
Substances
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Escherichia coli Proteins
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Flavins
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Flavoproteins
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Dimethylallyltranstransferase
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3-octaprenyl-4-hydroxybenzoate carboxy-lyase
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Carboxy-Lyases
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ubiX protein, E coli