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Literature summary for 2.5.1.74 extracted from

  • Saito, Y.; Ogura, K.
    Biosynthesis of menaquinones. Enzymic prenylation of 1,4-dihydroxy-2-naphthoate by Micrococcus luteus membrane fractions (1981), J. Biochem., 89, 1445-1452.
    View publication on PubMed
Search for more literature for 2.5.1.74

Activating Compound

Activating Compound Comment Organism Structure
EDTA maximal activity at 5 mM, inhibition by 20 mM Micrococcus luteus

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
 Micrococcus luteus
EDTA maximal activity at 5 mM, inhibition by 20 mM. Mg2+ reactivates Micrococcus luteus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Micrococcus luteus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activation Micrococcus luteus
Mn2+ activation, less efficient than Mg2+ Micrococcus luteus

Organism

Organism UniProt Comment Textmining
Micrococcus luteus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate + 1,4-dihydroxy-2-naphthoate
-
 Micrococcus luteus demethylmenaquinone-3 + phosphate + CO2
-
 ?
farnesyl diphosphate + 1,4-dihydroxy-3-methyl-2-naphthoate
-
 Micrococcus luteus methylmenaquinone-3 + phosphate + CO2
-
 ?
farnesyl diphosphate + 1-hydroxy-2-naphthoate
-
 Micrococcus luteus 2-farnesyl-1-naphthol + phosphate + CO2
-
 ?
farnesyl diphosphate + 2-carboxy-4-hydroxy-alpha-tetralone
-
 Micrococcus luteus demethylmenaquinone-3 + phosphate + CO2
-
 ?
additional information prenyl diphosphates ranging in chain length from C15 to C45 are active as substrates, as are monophosphate esters. Enzyme is specific for the aromatic substrate. Neither 1,4-dihydroxynaphthalene nor its 2-methyl derivative is substrate. Farnesyl diphosphate is the best prenyl donor Micrococcus luteus ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Micrococcus luteus