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Literature summary for 2.5.1.122 extracted from

  • Yu, X.; Xie, X.; Li, S.M.
    Substrate promiscuity of secondary metabolite enzymes: prenylation of hydroxynaphthalenes by fungal indole prenyltransferases (2011), Appl. Microbiol. Biotechnol., 92, 737-748.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + L-tyrosine Leptosphaeria maculans
-
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
?

Organism

Organism UniProt Comment Textmining
Leptosphaeria maculans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + L-tyrosine
-
Leptosphaeria maculans diphosphate + 4-O-dimethylallyl-L-tyrosine
-
?
additional information no activity with 1-naphthol, 1,6-dihydroxynaphthalene, 1,7-dihydroxynaphthalene, 2,6-dihydroxynaphthalene, 2,7-dihydroxynaphthalene, 3,5-dihydroxy-2-naphthoic acid, and 3,7-dihydroxy-2-naphthoic acid Leptosphaeria maculans ?
-
?

Synonyms

Synonyms Comment Organism
SirD
-
Leptosphaeria maculans
tyrosine O-prenyltransferase
-
Leptosphaeria maculans