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Information on EC 1.14.99.60 - 3-demethoxyubiquinol 3-hydroxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P41735

for references in articles please use BRENDA:EC1.14.99.60
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IUBMB Comments
The enzyme catalyses the last hydroxylation reaction during the biosynthesis of ubiquinone.
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Saccharomyces cerevisiae
UNIPROT: P41735
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
clk-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-methoxy-3-methyl-2-(all-trans-polyprenyl)-1,4-benzoquinol 5-hydroxylase
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clk-1
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COQ7
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ubiF
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SYSTEMATIC NAME
IUBMB Comments
6-methoxy-3-methyl-2-(all-trans-polyprenyl)-1,4-benzoquinol,acceptor:oxygen oxidoreductase (5-hydroxylating)
The enzyme catalyses the last hydroxylation reaction during the biosynthesis of ubiquinone.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-methoxy-3-methyl-2-(all-trans-polyprenyl)-1,4-benzoquinol + a reduced acceptor + O2
3-demethylubiquinol + acceptor + H2O
show the reaction diagram
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-methoxy-3-methyl-2-(all-trans-polyprenyl)-1,4-benzoquinol + a reduced acceptor + O2
3-demethylubiquinol + acceptor + H2O
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
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the Escherichia coli UbiF gene expressed at low copy restores growth of Coq7 point mutant E194K on medium containing a non-fermentable carbon source, but fails to rescue a coq7 null mutant. Expression of UbiF from a multicopy vector restores growth and coenzyme Q synthesis for both mutants, although with a higher efficiency in the point mutant. Addition of coenzyme Q to the growth media also stabilizes the Coq3 and Coq4 polypeptides in the coq7 null mutant
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E194K
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mutation affects invariant residue predicted to function as ligands to the di-iron center. Mutant is respiratory defective, lacks coenzyme Q6, and accumulates relatively large amounts of demethoxycoenzyme Q6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marbois, B.; Clarke, C.
The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis
J. Biol. Chem.
271
2995-3004
1996
Saccharomyces cerevisiae (P41735)
Manually annotated by BRENDA team
Jonassen, T.; Davis, D.E.; Larsen, P.L.; Clarke, C.F.
Reproductive fitness and quinone content of Caenorhabditis elegans clk-1 mutants fed coenzyme Q isoforms of varying length
J. Biol. Chem.
278
51735-51742
2003
Saccharomyces cerevisiae (P41735)
Manually annotated by BRENDA team
Tran, U.; Marbois, B.; Gin, P.; Gulmezian, M.; Jonassen, T.; Clarke, C.
Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide Two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis
J. Biol. Chem.
281
16401-16409
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team