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Literature summary for 2.5.1.80 extracted from

  • Fan, A.; Zocher, G.; Stec, E.; Stehle, T.; Li, S.M.
    Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme (2015), J. Biol. Chem., 290, 1364-1373.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus
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diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
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?

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus Q4WYG3
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + L-tryptophan
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Aspergillus fumigatus diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
?
dimethylallyl diphosphate + L-tryptophan the enzyme catalyzes C7-prenylation of the indole ring Aspergillus fumigatus diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
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?
additional information enzyme 7-DMATS also accepts L-tyrosine as substrate and converts it to an O-prenylated derivative, cf. EC 2.5.1.122. 7-DMATS is also able to take L-tyrosine and two derivatives thereof as substrates and catalyzes the same O- or N-prenylation Aspergillus fumigatus ?
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?

Synonyms

Synonyms Comment Organism
7-dimethylallyl tryptophan synthase
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Aspergillus fumigatus
7-DMATS
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Aspergillus fumigatus