Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kremer, A.; Li, S.M.
    A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL (2010), Microbiology, 156, 278-286.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.122 overexpression in Escherichia coli Leptosphaeria maculans

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.122 EDTA 5 mM, 12% inhibition Leptosphaeria maculans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.122 0.13
-
 L-tyrosine pH 7.5, 37°C Leptosphaeria maculans
2.5.1.122 0.17
-
 dimethylallyl diphosphate pH 7.5, 37°C Leptosphaeria maculans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.122 Ca2+ 5 mM, 1.4fold activation compared to activity without additives Leptosphaeria maculans
2.5.1.122 additional information no requirement for divalent metal ion Leptosphaeria maculans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.122 50000
-
 2 * 50000, SDS-PAGE Leptosphaeria maculans
2.5.1.122 100000
-
 His6-tagged enzyme, gel filtration Leptosphaeria maculans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.122 dimethylallyl diphosphate + L-tyrosine Leptosphaeria maculans the enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL diphosphate + 4-O-dimethylallyl-L-tyrosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.122 Leptosphaeria maculans Q6Q874
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.122
-
 Leptosphaeria maculans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.122 dimethylallyl diphosphate + L-3,4-dihydroxyphenylalanine 16.6% of the activity, compared to L-tyrosine. It is expected that the prenylation takes place at the 4-hydroxyl group. The structure of the product is not determined Leptosphaeria maculans ?
-
 ?
2.5.1.122 dimethylallyl diphosphate + L-tyrosine the enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL Leptosphaeria maculans diphosphate + 4-O-dimethylallyl-L-tyrosine
-
 ?
2.5.1.122 dimethylallyl diphosphate + L-tyrosine no activity with cyclo-L-Tyr-L-Ser, L-Phe, 4-hydroxybenzoate or 4-coumarate Leptosphaeria maculans diphosphate + 4-O-dimethylallyl-L-tyrosine
-
 ?
2.5.1.122 additional information SirD also prenylates L-Trp, resulting in the formation of 7-dimethylallyltryptophan. SirD catalyses the C-prenylation of L-Trp, in addition to the O-prenylation of L-Tyr, cf. EC 2.5.1.34 Leptosphaeria maculans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.122 dimer 2 * 50000, SDS-PAGE Leptosphaeria maculans

Synonyms

EC Number Synonyms Comment Organism
2.5.1.122 SirD
-
 Leptosphaeria maculans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.122 37
-
 assay at Leptosphaeria maculans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.122 1
-
 L-tyrosine pH 7.5, 37°C Leptosphaeria maculans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.122 7.5
-
 assay at Leptosphaeria maculans

General Information

EC Number General Information Comment Organism
2.5.1.122 physiological function the enzyme is involved in biosynthesis of the epidithiopiperazinedione toxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans Leptosphaeria maculans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.122 7.7
-
 L-tyrosine pH 7.5, 37°C Leptosphaeria maculans