EC Number   |
General Information |
Reference |
|---|
   2.5.1.80 | evolution |
the enzyme belongs to the DMATS superfamily |
721373 |
| 2.5.1.80 | evolution |
the enzyme belongs to the DMATS superfamily, 7-DMATS has a more flexible substrate specificity towards flavonoid compounds than other fungal prenyltransferases |
722044 |
| 2.5.1.80 | evolution |
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 |
723104 |
| 2.5.1.80 | evolution |
the enzyme is a member of the DMATS superfamily |
729072 |
| 2.5.1.80 | evolution |
the enzyme is part of the DMATS superfamily |
737544, 739221 |
| 2.5.1.80 | metabolism |
the enzyme is involved in the biosynthesis of astechrome |
739221 |
| 2.5.1.80 | more |
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 |
737837 |
| 2.5.1.80 | physiological function |
the enzyme is involved in the biosynthesis of astechrome in Aspergillus fumigatus |
-, 737407 |
