2.5.1.80: 7-dimethylallyltryptophan synthase
This is an abbreviated version!
For detailed information about 7-dimethylallyltryptophan synthase, go to the full flat file.
Word Map on EC 2.5.1.80
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2.5.1.80
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prenylation
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indole
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drug development
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dmapp
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fumigatus
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o-prenyltransferase
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synthesis
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regioselective
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dipeptide
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fgapt2
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his6-fusion
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o-prenylated
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c-prenylations
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maculans
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leptosphaeria
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neosartorya
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tryptophan-containing
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biotechnology
- 2.5.1.80
-
prenylation
- indole
- drug development
-
dmapp
- fumigatus
-
o-prenyltransferase
- synthesis
-
regioselective
- dipeptide
- fgapt2
-
his6-fusion
-
o-prenylated
-
c-prenylations
- maculans
-
leptosphaeria
- neosartorya
-
tryptophan-containing
- biotechnology
Reaction
Synonyms
7-dimethylallyl tryptophan synthase, 7-dimethylallyltryptophan synthase, 7-DMATS, 7-DMATSNeo, ANI_1_660114, CAK41583, dimethylallyltryptophan synthase, tryptophan C7-prenyltransferase
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General Information
General Information on EC 2.5.1.80 - 7-dimethylallyltryptophan synthase
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evolution
metabolism
the enzyme is involved in the biosynthesis of astechrome
physiological function
additional information
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analysis of the structural basis of the regioselective prenylation of L-tryptophan at the C7 position by comparison of the three-dimensional structural models of 7-DMATSNeo with FgaPT2 (4-DMATS), EC 2.5.1.34, from Aspergillus fumigatus. Construction of three-dimensional structural models of 7 DMATSNeo and FgaPT2 (4-DMATS). Docking studies of potential substrates, overview. Residues F129, L130, E138, F226, F243 are involved in binding of L-tryptophan, residue Y393 is involved in stabilization of the allylic cation via cation-Pi interactions. Residues R154, K239, Y241, R311, K313, K391, Y393, K454, and Y460 are involved in diphosphate coordination
evolution
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the enzyme belongs to the DMATS superfamily, 7-DMATS has a more flexible substrate specificity towards flavonoid compounds than other fungal prenyltransferases
evolution
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the enzyme belongs to the DMATS superfamily. The members of the DMATS superfamily contain no DDxxD motifs, which are essential for binding of prenyl diphosphate via metal ions, for example, Mg2+ or Mn2+, in trans prenyltransferases
evolution
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the enzyme belongs to the DMATS superfamily. The members of the DMATS superfamily contain no DDxxD motifs, which are essential for binding of prenyl diphosphate via metal ions, for example, Mg2+ or Mn2+, in trans prenyltransferases
the enzyme is involved in the biosynthesis of astechrome in Aspergillus fumigatus
physiological function
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the enzyme is involved in the biosynthesis of astechrome in Aspergillus fumigatus
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