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Literature summary extracted from

  • Nakahigashi, K.; Miyamoto, K.; Nishimura, K.; Inokuchi, H.
    Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone (1992), J. Bacteriol., 174, 7352-7359.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.99.B5
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Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.B5 Escherichia coli P25534
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.B5 2-methoxy-6-(all-trans-octaprenyl)phenol + a reduced electron acceptor + oxygen no direct biochemical evidence for the enzymatic activity. Based on information obtained from studies with ubiquinone-deficient mutants, a pathway is proposed for ubiquinone biosynthesis in Escherichia coli. ubiH mutants accumulate small quantities of 2-octaprenyl-6-methoxyphenol and relatively large amounts of 2-octaprenylphenol Escherichia coli 6-all-trans-octaprenyl-2-methoxy-1,4-benzoquinol + a reduced electron acceptor + H2O
-
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Synonyms

EC Number Synonyms Comment Organism
1.14.99.B5 ubiH
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Escherichia coli
1.14.99.B5 visB
-
Escherichia coli

General Information

EC Number General Information Comment Organism
1.14.99.B5 malfunction mutation that is lethal when the cells are exposed to visible light. The photosensitive phenotype appears to be due to the accumulation of the substrate for the reaction catalyzed by the visB (ubiH) gene product Escherichia coli
1.14.99.B5 malfunction ubiH mutants accumulate small quantities of 2-octaprenyl-6-methoxyphenol and relatively large amounts of 2-octaprenylphenol Escherichia coli
1.14.99.B5 physiological function the enzyme catalyzes a reaction in the ubiquinone biosynthesis pathway Escherichia coli