ExplorEnz: EC 1.97.1.15

Your query returned 1 entry. Printable version

1.97.1.15

Accepted name:

2-(all-trans-polyprenyl)phenol 6-hydroxylase (prephenate)

Reaction:

(1) a 2-(all-trans-polyprenyl)phenol + prephenate + acceptor = a 3-(all-trans-polyprenyl)benzene-1,2-diol + 3-phenyl-2-oxopropanoate + CO₂ + reduced acceptor
(2) a 2-methoxy-6-(all-trans-polyprenyl)phenol + prephenate + acceptor = a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol + 3-phenyl-2-oxopropanoate + CO₂ + reduced acceptor
(3) a 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol + prephenate + acceptor = a 3-demethylubiquinol + 3-phenyl-2-oxopropanoate + CO₂ + reduced acceptor

Glossary:

3-phenyl-2-oxopropanoate = phenylpyruvate

Other name(s):

ubiquinone hydroxylase UbiUV

Systematic name:

prephenate,acceptor:2-(all-trans-polyprenyl)phenol oxidoreductase (6-hydroxylating)

Comments:

The enzyme, characterized from the bacterium Escherichia coli, catalyses three hydroxylation reactions in the oxygen-independent pathway for ubiquinone (UQ) biosynthesis. The reaction involves an electron acceptor whose identity remains unknown as of 2024. The Escherichia coli enzyme is a heterodimer, with both subunits containing a [4Fe-4S] cluster that is essential for activity and may serve as part of an electron transfer chain from the substrate to the unidentified electron acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Pelosi, L., Vo, C.D., Abby, S.S., Loiseau, L., Rascalou, B., Hajj Chehade, M., Faivre, B., Gousse, M., Chenal, C., Touati, N., Binet, L., Cornu, D., Fyfe, C.D., Fontecave, M., Barras, F., Lombard, M. and Pierrel, F. Ubiquinone biosynthesis over the entire O₂ range: Characterization of a conserved O₂-independent pathway. mBio 10 (2019) . [DOI] [PMID: 31289180]
2.	Arias-Cartin, R., Kazemzadeh Ferizhendi, K., Sechet, E., Pelosi, L., Loeuillet, C., Pierrel, F., Barras, F. and Bouveret, E. Role of the Escherichia coli ubiquinone-synthesizing UbiUVT pathway in adaptation to changing respiratory conditions. mBio 14:e0329822 (2023). [DOI] [PMID: 37283518]
3.	Ferizhendi, K.K., Simon, P., Pelosi, L., Sechet, E., Arulanandam, R., Chehade, M.H., Rey, M., Onal, D., Flandrin, L., Chreim, R., Faivre, B., Vo, S.C., Arias-Cartin, R., Barras, F., Fontecave, M., Bouveret, E., Lombard, M. and Pierrel, F. An organic O donor for biological hydroxylation reactions. Proc. Natl. Acad. Sci. USA 121:e2321242121 (2024). [DOI] [PMID: 38507448]

[EC 1.97.1.15 created 2024]