2.5.1.106: tryprostatin B synthase
This is an abbreviated version!
For detailed information about tryprostatin B synthase, go to the full flat file.
Word Map on EC 2.5.1.106
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2.5.1.106
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prenylation
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aspergillus
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fumigatus
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dipeptides
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tryptophan-containing
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dimethylallyltryptophan
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cyclo-l-trp-l-pro
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tryprostatins
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regiospecific
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dmapp
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regioselectivity
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fumitremorgins
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7-dmats
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chemoenzymatic
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anapt
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diketopiperazine
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cdpnpt
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barrel
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actinomycetes
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isoprenoid
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coelicolor
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l-tryptophan
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fischeri
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neosartorya
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ergot
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fgapt2
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l-trp
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medicine
- 2.5.1.106
-
prenylation
- aspergillus
- fumigatus
- dipeptides
-
tryptophan-containing
- dimethylallyltryptophan
- cyclo-l-trp-l-pro
-
tryprostatins
-
regiospecific
-
dmapp
-
regioselectivity
-
fumitremorgins
- 7-dmats
-
chemoenzymatic
- anapt
-
diketopiperazine
- cdpnpt
-
barrel
- actinomycetes
-
isoprenoid
- coelicolor
- l-tryptophan
- fischeri
-
neosartorya
-
ergot
- fgapt2
- l-trp
- medicine
Reaction
Synonyms
brevianamide F prenyltransferase, cyclic dipeptide C2-prenyltransferase FtmPT1, FtmPT1, indole prenyltransferase, tryprostatin B synthase
ECTree
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medicine
enzyme converts tryptophan-containing cyclic dipeptides to their C2-regularly prenylated derivatives. In human leukemia K562 and ovarian cancer A2780 sens and A2780 CisR cell lines, prenylation at C2 leads to a significant increase of the cytotoxicity of the tested cyclic dipeptides in all the 14 cases
medicine
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enzyme converts tryptophan-containing cyclic dipeptides to their C2-regularly prenylated derivatives. In human leukemia K562 and ovarian cancer A2780 sens and A2780 CisR cell lines, prenylation at C2 leads to a significant increase of the cytotoxicity of the tested cyclic dipeptides in all the 14 cases
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