2.5.1.B31: 5-dimethylallyltryptophan synthase
This is an abbreviated version!
For detailed information about 5-dimethylallyltryptophan synthase, go to the full flat file.
Word Map on EC 2.5.1.B31
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2.5.1.B31
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indole
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synthesis
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7-dmats
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fgapt2
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dmapp
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actinomycete
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chemoenzymatic
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regioselectivity
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coelicolor
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dimethylallyltryptophans
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regiospecific
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geranyl
- 2.5.1.B31
- indole
- synthesis
- 7-dmats
- fgapt2
-
dmapp
-
actinomycete
-
chemoenzymatic
-
regioselectivity
- coelicolor
- dimethylallyltryptophans
-
regiospecific
-
geranyl
Reaction
Synonyms
5-DMATS, 5-DMATSSc, C5-prenyltransferase, dimethylallyl-tryptophan synthase, EAW08391, SCO7467, tryptophan C5-prenyltransferase
ECTree
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General Information
General Information on EC 2.5.1.B31 - 5-dimethylallyltryptophan synthase
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evolution
metabolism
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enzyme 5-DMATSSc enzyme is involved in biosynthesis of dimethylallylindole 3-acetonitrile
additional information
5-DMATS belongs to the DMATS superfamily, indole prenyltransferases with different prenylation positions, overview
evolution
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the enzyme belongs to the dimethylallyl-tryptophan synthase, DMATS, superfamily
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
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
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molecular dynamics simulation experiments with a homologous model of 5-DMATS, overview
additional information
molecular dynamics simulation experiments with a homologous model of 5-DMATS, overview
additional information
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possibility of producing prenylated analogues of ardeemin fumiquinazoline, a precursor of the multidrug resistance (MDR) export pump inhibitor ardeemin, by using dimethylallydiphosphate transferase enzymes, e.g. 5-DMATSSc
additional information
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molecular dynamics simulation experiments with a homologous model of 5-DMATS, overview
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