The Enzyme Database

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EC 1.13.11.83     
Accepted name: 4-hydroxy-3-prenylphenylpyruvate oxygenase
Reaction: 3-(4-hydroxy-3-prenylphenyl)pyruvate + O2 = 4-hydroxy-3-prenylmandelate + CO2
For diagram of 3-dimethylallyl-4-hydroxybenzoate biosynthesis, click here
Glossary: 3-(4-hydroxy-3-prenylphenyl)pyruvate = 3-(4-hydroxy-3-prenylphenyl)-2-oxopropanoate
4-hydroxy-3-prenylmandelate = 2-hydroxy-2-(4-hydroxy-3-prenylphenyl)acetate
prenyl = 3-methylbut-2-en-1-yl
Other name(s): CloR
Systematic name: 3-(4-hydroxy-3-prenylphenyl)pyruvate:oxygen 1,2-oxidoreductase (4-hydroxy-3-prenylmandelate-forming)
Comments: Requires non-heme-iron(II). Isolated from the bacterium Streptomyces roseochromogenes DS 12976. A bifunctional enzyme involved in clorobiocin biosynthesis that also catalyses the activity of EC 1.13.12.23, 4-hydroxy-3-prenylbenzoate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pojer, F., Kahlich, R., Kammerer, B., Li, S.M. and Heide, L. CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis. J. Biol. Chem. 278 (2003) 30661–30668. [DOI] [PMID: 12777382]
[EC 1.13.11.83 created 2017]
 
 
EC 2.5.1.111     
Accepted name: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Reaction: prenyl diphosphate + 3-(4-hydroxyphenyl)pyruvate = diphosphate + 3-(4-hydroxy-3-prenylphenyl)pyruvate
For diagram of 3-dimethylallyl-4-hydroxybenzoate biosynthesis, click here and for diagram of 4-hydroxyphenylpyruvate metabolites, click here
Glossary: 3-dimethylallyl-4-hydroxyphenylpyruvate = 3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]-2-oxopropanoate
Other name(s): CloQ; 4HPP dimethylallyltransferase; NovQ; dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Systematic name: prenyl-diphosphate:3-(4-hydroxyphenyl)pyruvate 3′-prenyltransferase
Comments: The enzyme's product feeds into the biosynthesis of the aminocoumarin antibiotics clorobiocin and novobiocin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pojer, F., Wemakor, E., Kammerer, B., Chen, H., Walsh, C.T., Li, S.M. and Heide, L. CloQ, a prenyltransferase involved in clorobiocin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 2316–2321. [DOI] [PMID: 12618544]
2.  Keller, S., Pojer, F., Heide, L. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1153–1155. [DOI] [PMID: 17077503]
3.  Metzger, U., Keller, S., Stevenson, C.E., Heide, L. and Lawson, D.M. Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J. Mol. Biol. 404 (2010) 611–626. [DOI] [PMID: 20946900]
4.  Ozaki, T., Mishima, S., Nishiyama, M. and Kuzuyama, T. NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids. J. Antibiot. (Tokyo) 62 (2009) 385–392. [DOI] [PMID: 19557032]
[EC 2.5.1.111 created 2013]
 
 


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