EC 4.1.1.98 - 4-hydroxy-3-polyprenylbenzoate decarboxylase
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ENZYME view
IntEnz Enzyme Nomenclature
EC 4.1.1.98
Names
Accepted name:
4-hydroxy-3-polyprenylbenzoate decarboxylase
Other
names:
ubiD (gene name)
4-hydroxy-3-solanesylbenzoate decarboxylase
3-octaprenyl-4-hydroxybenzoate decarboxylase
4-hydroxy-3-solanesylbenzoate decarboxylase
3-octaprenyl-4-hydroxybenzoate decarboxylase
Systematic name:
4-hydroxy-3-polyprenylbenzoate carboxy-lyase
Reaction
- a 4-hydroxy-3-polyprenylbenzoate = a 2-polyprenylphenol + CO2
Comments:
The enzyme catalyses a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.
Links to other databases
Gene Ontology:
GO:0008694
References
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Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase.Biochim. Biophys. Acta 436 : 800-810 (1976). [PMID: 782527]
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The role of UbiX in Escherichia coli coenzyme Q biosynthesis.Arch. Biochem. Biophys. 467 : 144-153 (2007). [PMID: 17889824]
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Chorismate pyruvate-lyase and 4-hydroxy-3-solanesylbenzoate decarboxylase are required for plastoquinone biosynthesis in the cyanobacterium Synechocystis sp. PCC6803.J. Biol. Chem. 289 : 2675-2686 (2014). [PMID: 24337576]
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Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase.ACS Chem. Biol. (2015). [PMID: 25647642]
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New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition.Nature 522 : 497-501 (2015). [PMID: 26083754]
[EC 4.1.1.98 created 2014, modified 2015]