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
-
aspergillus
-
fumigatus
-
dipeptides
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tryptophan-containing
-
dimethylallyltryptophan
-
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
-
7-dmats
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chemoenzymatic
-
anapt
-
diketopiperazine
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cdpnpt
-
barrel
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actinomycetes
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isoprenoid
-
coelicolor
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l-tryptophan
-
fischeri
-
neosartorya
-
ergot
-
fgapt2
-
l-trp
-
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
2.5.1.106 tryprostatin B synthaseAdvanced search results
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results (Crystallization
Crystallization on EC 2.5.1.106 - tryprostatin B synthase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
crystal structures of unliganded enzyme FtmPT1 to 2.5 A resolution as well as of a ternary complex of FtmPT1 bound to brevianamide F and an analogue of its isoprenoid substrate dimethylallyl diphosphate. FtmPT1 assumes a rare alpha/beta-barrel fold, consisting of 10 circularly arranged -strands surrounded by alpha-helices. Catalysis is performed in a hydrophobic reaction chamber at the center of the barrel
