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Information on EC 2.5.1.106 - tryprostatin B synthase
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2.5.1.106 tryprostatin B synthaseIUBMB Comments
The enzyme from the fungus Aspergillus fumigatus can also prenylate other tryptophan-containing cyclic dipeptides. Prenylation occurs mainly at C-2 , but also at C-3 . Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, cyclotryprostatins, spirotryprostatins, fumitremorgins and verruculogen.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Aspergillus subgen. Fumigati
Synonyms
indole prenyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
brevianamide F prenyltransferase
-
-
ambiguous
-
FtmPT1
indole prenyltransferase
FtmPT1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + brevianamide F = diphosphate + tryprostatin B
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:brevianamide-F dimethylallyl-C-2-transferase
The enzyme from the fungus Aspergillus fumigatus can also prenylate other tryptophan-containing cyclic dipeptides. Prenylation occurs mainly at C-2 [1], but also at C-3 [2]. Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, cyclotryprostatins, spirotryprostatins, fumitremorgins and verruculogen.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,6-dihydroxynaphthalene + dimethylallyl diphosphate
diphosphate + 4-(3-methylbut-2-en-1-yl)naphthalene-1,6-diol
-
mutants Y205L, Y205M, Y205F, Y205C, Y205I, Y205S, and G115A_Y205C show higher catalytic activities than the non-mutated FtmPT1
-
-
?
1,7-dihydroxynaphthalene + dimethylallyl diphosphate
diphosphate + 4-(3-methylbut-2-en-1-yl)naphthalene-1,7-diol
-
mutants Y205L, Y205M, Y205F, Y205C, Y205I, Y205S, and G115A_Y205C show higher catalytic activities than the non-mutated FtmPT1
-
-
?
1-amino-7-hydroxynaphthalene + dimethylallyl diphosphate
diphosphate + 8-amino-7-(3-methylbut-2-en-1-yl)naphthalen-2-ol
-
mutants Y205L, Y205M, Y205F, Y205C, Y205I, Y205S, and G115A_Y205C show higher catalytic activities than the non-mutated FtmPT1
-
-
?
1-naphthol + dimethylallyl diphosphate
diphosphate + 4-(3-methylbut-2-en-1-yl)naphthalen-1-ol
-
mutants Y205L, Y205M, Y205F, Y205C, Y205I, Y205S, and G115A_Y205C show higher catalytic activities than the non-mutated FtmPT1
-
-
?
2,3-dihydroxynaphthalene + dimethylallyl diphosphate
diphosphate + ?
-
mutants Y205L, Y205M, Y205F, Y205C, Y205I, Y205S, and G115A_Y205C show higher catalytic activities than the non-mutated FtmPT1
-
-
?
2-naphthol + dimethylallyl diphosphate
diphosphate + ?
-
mutants Y205L, Y205M, Y205F, Y205C, Y205I, Y205S, and G115A_Y205C show higher catalytic activities than the non-mutated FtmPT1
-
-
?
brevianamide F + dimethylallyl diphosphate
diphosphate + tryprostatin B
-
-
-
-
?
dimethylallyl diphosphate + (E)-4-(1H-indol-3-yl)but-3-en-2-one
diphosphate + (3E)-3-(1H-indol-3-ylmethylidene)-6-methylhept-5-en-2-one
dimethylallyl diphosphate + 2-methylbrevianamide F
diphosphate + ?
-
i.e. cyclo-L-2-methyltryptophan-L-proline
-
-
?
dimethylallyl diphosphate + 5-hydroxybrevianamide F
diphosphate + ?
-
i.e. cyclo-L-5-hydroxytryptophan-L-proline
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + (2S,3aR,8aR)-3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
dimethylallyl diphosphate + brevianamide F
diphosphate + (5aS,6aR,11aR,13aS)-6a-(3-methylbut-2-en-1-yl)-2,3,6,6a,11,11a-hexahydro-1H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-5,13(5aH,13aH)-dione
dimethylallyl diphosphate + brevianamide F
diphosphate + (5aS,6aR,11aS,13aS)-6a-(2-methylbut-3-en-2-yl)-2,3,6,6a,11,11a-hexahydro-1H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-5,13(5aH,13aH)-dione + tryprostatin B
the reaction occurs with mutant enzyme G115T
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-D-Ala)
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-D-Pro)
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-D-Pro)
dimethylallyl diphosphate + cyclo-(D-Trp-L-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Ala)
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-L-Pro)
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-Trp-L-Pro)
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Pro)
dimethylallyl diphosphate + cyclo-(L-Trp-D-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-D-Ala)
dimethylallyl diphosphate + cyclo-(L-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-L-Trp-D-Pro)
dimethylallyl diphosphate + cyclo-(L-Trp-D-Pro)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-D-Pro)
product yield 75.7%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-Gly)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-Gly)
dimethylallyl diphosphate + cyclo-(L-Trp-L-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Ala)
dimethylallyl diphosphate + cyclo-(L-Trp-L-His)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-His)
dimethylallyl diphosphate + cyclo-(L-Trp-L-Leu)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Leu)
dimethylallyl diphosphate + cyclo-(L-Trp-L-Phe)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Phe)
dimethylallyl diphosphate + cyclo-(L-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-Trp-L-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Trp)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Trp)
dimethylallyl diphosphate + cyclo-(L-Trp-L-Tyr)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Tyr)
dimethylallyl diphosphate + cyclo-L-2-methyltryptophan-L-proline
diphosphate + (5aS,6aS,13aS)-6a-(3-methylbut-2-en-1-yl)-2,3,6,6a,11,11a-hexahydro-1H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-5,13(5aH,13aH)-dione
-
i.e. 2-methylbrevianamide F
product is a normal prenylated hexahydropyrroloindole that contains a substituent at C-3 and has cyclized. An N-1 normal prenylated product is formed as minor product
-
?
dimethylallyl diphosphate + DL-4-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-4-methyl-tryptophan
dimethylallyl diphosphate + DL-6-fluoro-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-6-fluoro-tryptophan
dimethylallyl diphosphate + DL-6-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-6-methyl-tryptophan
dimethylallyl diphosphate + DL-7-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-7-methyl-tryptophan
-
conversion rate 24.3%
-
?
dimethylallyl diphosphate + L-Nalpha-methyl-tryptophan
diphosphate + L-1-(3'-dimethylallyl)-Nalpha-methyl-tryptophan
-
conversion rate 11.1%
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + (2S,3aR,8aR)-3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
-
-
18% conversion after extended incubation, product is a hexahydropyrroloindole that results from reverse C-3 prenylation followed by ring closure
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + L-1-(3'-dimethylallyl)-tryptophan
-
conversion rate 37.8%
-
?
dimethylallylphosphate + cyclo-L-5-hydroxytryptophan-L-proline
diphosphate + (3S,8aS)-3-[[5-hydroxy-4-(3-methylbut-2-en-1-yl)-2,3-dihydro-1H-indol-3-yl]methyl]hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
-
i.e. 5-hydroxybrevianamide F
product is formed by normal prenylation in C-4 position
-
?
dimethylallyl diphosphate + (E)-4-(1H-indol-3-yl)but-3-en-2-one
diphosphate + (3E)-3-(1H-indol-3-ylmethylidene)-6-methylhept-5-en-2-one
-
46% yield
-
?
dimethylallyl diphosphate + (E)-4-(1H-indol-3-yl)but-3-en-2-one
diphosphate + (3E)-3-(1H-indol-3-ylmethylidene)-6-methylhept-5-en-2-one
-
46% yield
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + (2S,3aR,8aR)-3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
-
product of mutant G115T, no product of wild-type
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + (2S,3aR,8aR)-3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
-
product of mutant G115T, no product of wild-type
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + (5aS,6aR,11aR,13aS)-6a-(3-methylbut-2-en-1-yl)-2,3,6,6a,11,11a-hexahydro-1H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-5,13(5aH,13aH)-dione
-
product of Tyr205 mutants, no product of wild-type
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + (5aS,6aR,11aR,13aS)-6a-(3-methylbut-2-en-1-yl)-2,3,6,6a,11,11a-hexahydro-1H-pyrrolo[1'',2'':4',5']pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-5,13(5aH,13aH)-dione
-
product of Tyr205 mutants, no product of wild-type
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
mutant G115T catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
catalyzes the prenylation of cyclo-L-Trp-L-Pro , i.e.brevianamide F, at the C-2 position of the indole nucleus
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
i.e. cyclo-(L-Trp-L-Pro)
82.3% yield of C2-prenylated product, plus 0.7% C3-prenylated product
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
i.e. cyclo-L-Trp-L-Pro
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
mutant G115T catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
catalyzes the prenylation of cyclo-L-Trp-L-Pro , i.e.brevianamide F, at the C-2 position of the indole nucleus
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
i.e. cyclo-(L-Trp-L-Pro)
82.3% yield of C2-prenylated product, plus 0.7% C3-prenylated product
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-D-Ala)
product yield 8.3%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-D-Ala)
product yield 8.3%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-D-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-D-Pro)
product yield 27.4%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-D-Pro)
product yield 27.4%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-D-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-D-Pro)
43.4% yield of C2-prenylated product, plus 11.8% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-D-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-D-Pro)
43.4% yield of C2-prenylated product, plus 11.8% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Ala)
46.4% yield of C2-prenylated product, plus 11.6% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Ala)
product yield 46.4%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Ala)
product yield 46.4%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Ala)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Ala)
46.4% yield of C2-prenylated product, plus 11.6% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-L-Pro)
product yield 43.4%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-D-Trp-L-Pro)
product yield 43.4%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-Trp-L-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(2-dimethylallyl-Trp-L-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Pro)
32.6% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Pro)
product yield 82.3%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Pro)
product yield 82.3%
-
-
?
dimethylallyl diphosphate + cyclo-(D-Trp-L-Pro)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Pro)
32.6% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-D-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-D-Ala)
43.9% yield of C2-prenylated product, plus 12.1% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-D-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-D-Ala)
product yield 43.9%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-D-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-D-Ala)
43.9% yield of C2-prenylated product, plus 12.1% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-L-Trp-D-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-D-Pro)
diphosphate + cyclo-(2-dimethylallyl-L-Trp-D-Pro)
-
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-Gly)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-Gly)
4.7% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-Gly)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-Gly)
57% yield of C2-prenylated product, plus 18.6% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-Gly)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-Gly)
product yield 57.0%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-Gly)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-Gly)
4.7% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Ala)
53.5% yield of C2-prenylated product, plus 12.7% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Ala)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Ala)
product yield 53.5%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-His)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-His)
68.1% yield of C2-prenylated product, plus 6.8% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-His)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-His)
product yield 68.1%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Leu)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Leu)
21.9% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Leu)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Leu)
product yield 70.9%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Leu)
diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Leu)
21.9% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Phe)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Phe)
3.4% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Phe)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Phe)
product yield 39.3%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Trp)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Trp)
6.4% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Trp)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Trp)
product yield 67.0%
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Tyr)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Tyr)
5.0% of the activity with brevianamide F
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Tyr)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Tyr)
72.4% yield of C2-prenylated product, plus 1.1% C3-prenylated product
-
-
?
dimethylallyl diphosphate + cyclo-(L-Trp-L-Tyr)
diphosphate + cyclo-(L-2-dimethylallyl-Trp-L-Tyr)
product yield 72.4%
-
-
?
dimethylallyl diphosphate + DL-4-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-4-methyl-tryptophan
-
conversion rate 7.3%
-
?
dimethylallyl diphosphate + DL-4-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-4-methyl-tryptophan
-
conversion rate 7.3%
-
?
dimethylallyl diphosphate + DL-6-fluoro-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-6-fluoro-tryptophan
-
conversion rate 21%
-
?
dimethylallyl diphosphate + DL-6-fluoro-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-6-fluoro-tryptophan
-
conversion rate 21%
-
?
dimethylallyl diphosphate + DL-6-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-6-methyl-tryptophan
-
conversion rate 36.3%
-
?
dimethylallyl diphosphate + DL-6-methyl-tryptophan
diphosphate + DL-1-(3'-dimethylallyl)-6-methyl-tryptophan
-
conversion rate 36.3%
-
?
additional information
?
-
enzyme catalyzes also regular C3-prenylation as side reaction. Prenylation products at C2 and C3 are independently formed during the enzyme reaction. Both C2- and C3-prenylations may begin simultaneously with the attack of the electron-rich indole ring at C2 and C33 to C1' of the dimethylallyl cation. Their ratio would be dependent on the position of a given aromatic substrate and accordingly the distance of C2 to C1' as well as C3 to C1'
-
-
?
additional information
?
-
enzyme shows a high substrate specificity towards dimethylallyl diphosphate, but accepts different tryptophan-containing cyclic dipeptides. No substrates: isopentenyl diphosphate or geranyl diphosphate
-
-
?
additional information
?
-
-
enzyme shows a high substrate specificity towards dimethylallyl diphosphate, but accepts different tryptophan-containing cyclic dipeptides. No substrates: isopentenyl diphosphate or geranyl diphosphate
-
-
?
additional information
?
-
in comparison to cyclic dipeptides, which are prenylated in a regular manner by FtmPT1 at C-2, tryptophan and its simple derivatives are prenylated reversely at N-1
-
-
?
additional information
?
-
no substrates: 4-hydroxybenzalacetone, benzalacetone, 3-indoleacrylic acid, 4-coumaric acid, cinnamic acid
-
-
?
additional information
?
-
-
no substrates: 4-hydroxybenzalacetone, benzalacetone, 3-indoleacrylic acid, 4-coumaric acid, cinnamic acid
-
-
?
additional information
?
-
the reaction is most likely initiated by hydrolysis of the phosphoric acid ester bond to form the dimethylallylic cation and a diphosphate group. The resulting carbocation would be stabilized from two sides by cation-pi interactions with aromatic ring systems, one from the substrate brevianamide F and one from the side chain of Y382. The stabilized cation can then undergo a nucleophilic attack from an aromatic nucleus such as that of the indole. The reactivity of the indole is likely enhanced by a hydrogen bond from its N-1 nitrogen to the side chain carboxylate of E102
-
-
?
additional information
?
-
-
the reaction is most likely initiated by hydrolysis of the phosphoric acid ester bond to form the dimethylallylic cation and a diphosphate group. The resulting carbocation would be stabilized from two sides by cation-pi interactions with aromatic ring systems, one from the substrate brevianamide F and one from the side chain of Y382. The stabilized cation can then undergo a nucleophilic attack from an aromatic nucleus such as that of the indole. The reactivity of the indole is likely enhanced by a hydrogen bond from its N-1 nitrogen to the side chain carboxylate of E102
-
-
?
additional information
?
-
-
a mechanism involving a C-3 normal prenylation as the first step of the catalysis. The barrier to the Cope rearrangement can be quite low, and it can readily proceed at room temperature in these biologically relevant systems. The slowest step in this nonenzymatic reaction might be ring opening of the hexahydropyrroloindole aminal
-
-
?
additional information
?
-
-
comparison of mechanisms of the indole alkaloid prenyltransferases. Tryprostatin B synthase catalyzes the normal C-2 prenylation of the indole ring in brevianamide F (cyclo-L-Trp-L-Pro). Mechanism includes an initial C-3 prenylation (either normal or reverse) followed by carbo cation rearrangements to give product
-
-
?
additional information
?
-
the C5-C8 and C2-C9 reaction channels have very similar activation parameters for the prenylation step. Hence, the final proton ransfer/cyclization step is the product-determining step, with the deprotonation of the C5-C8 intermediate being nearly without activation (0.5 kcal/mol), while the deprotonation process for the C2-C9 pathway has a substantial barrier (higher than the C5-C8 and C2-C9 intermediate states) of 16.8 kcal/mol, resulting in the exclusive formation of the wild-type product tryprostatin B. The diphosphate anion leaving group is stabilized throughout by Arg113, Lys201, Tyr205, Gln380, Lys294, Tyr450, and nine crystal water molecules in the active site
-
-
?
additional information
?
-
the reaction is most likely initiated by hydrolysis of the phosphoric acid ester bond to form the dimethylallylic cation and a diphosphate group. The resulting carbocation would be stabilized from two sides by cation-pi interactions with aromatic ring systems, one from the substrate brevianamide F and one from the side chain of Y382. The stabilized cation can then undergo a nucleophilic attack from an aromatic nucleus such as that of the indole. The reactivity of the indole is likely enhanced by a hydrogen bond from its N-1 nitrogen to the side chain carboxylate of E102
-
-
?
additional information
?
-
in comparison to cyclic dipeptides, which are prenylated in a regular manner by FtmPT1 at C-2, tryptophan and its simple derivatives are prenylated reversely at N-1
-
-
?
additional information
?
-
enzyme shows a high substrate specificity towards dimethylallyl diphosphate, but accepts different tryptophan-containing cyclic dipeptides. No substrates: isopentenyl diphosphate or geranyl diphosphate
-
-
?
additional information
?
-
enzyme catalyzes also regular C3-prenylation as side reaction. Prenylation products at C2 and C3 are independently formed during the enzyme reaction. Both C2- and C3-prenylations may begin simultaneously with the attack of the electron-rich indole ring at C2 and C33 to C1' of the dimethylallyl cation. Their ratio would be dependent on the position of a given aromatic substrate and accordingly the distance of C2 to C1' as well as C3 to C1'
-
-
?
additional information
?
-
no substrates: 4-hydroxybenzalacetone, benzalacetone, 3-indoleacrylic acid, 4-coumaric acid, cinnamic acid
-
-
?
additional information
?
-
the C5-C8 and C2-C9 reaction channels have very similar activation parameters for the prenylation step. Hence, the final proton ransfer/cyclization step is the product-determining step, with the deprotonation of the C5-C8 intermediate being nearly without activation (0.5 kcal/mol), while the deprotonation process for the C2-C9 pathway has a substantial barrier (higher than the C5-C8 and C2-C9 intermediate states) of 16.8 kcal/mol, resulting in the exclusive formation of the wild-type product tryprostatin B. The diphosphate anion leaving group is stabilized throughout by Arg113, Lys201, Tyr205, Gln380, Lys294, Tyr450, and nine crystal water molecules in the active site
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
brevianamide F + dimethylallyl diphosphate
diphosphate + tryprostatin B
-
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + tryprostatin B
-
i.e. cyclo-L-Trp-L-Pro
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.88
(E)-4-(1H-indol-3-yl)but-3-en-2-one
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
(E)-4-(1H-indol-3-yl)but-3-en-2-one
pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is involved in the biosynthesis of a number of biologically active natural products including tryprostatins, spirotryprostatins, verruculogen, and fumitremorgins
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FTMB_ASPFM
464
0
52607
Swiss-Prot
other Location (Reliability: 3)
FTMB_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
464
0
52607
Swiss-Prot
other Location (Reliability: 3)
FTMB_NEOFI
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)
463
0
52594
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E102Q
mutation reduces the production of tryprostatin B to undetectable amounts
G115A
G115A/Y205C
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
G115L
formation of tryprostatin B is abolished, formation of a new product occurs
G115T
Y205C
Y205D
mutant produces 55.8% C3-regularly prenylated product and 3.6% C3-reversely prenylated product
Y205E
mutant produces 57.6% C3-regularly prenylated product and 3% C3-reversely prenylated product
Y205F
Y205G
mutant produces 92% C3-regularly prenylated product and 12.2% C3-reversely prenylated product
Y205I
Y205K
mutant produces 110% C3-regularly prenylated product and 1.6% C3-reversely prenylated product
Y205L
Y205M
Y205N
mutant produces 70% C3-regularly prenylated product and 2.8% C3-reversely prenylated product
Y205R
mutant produces 77% C3-regularly prenylated product and 13.2% C3-reversely prenylated product
Y205S
E102Q
-
mutation reduces the production of tryprostatin B to undetectable amounts
-
G115L
-
formation of tryprostatin B is abolished, formation of a new product occurs
-
G115T
-
0.4% of wild-type activity in formation of trytrostatin B. Mutant catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus
-
G115A
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
G115T
0.4% of wild-type activity in formation of trytrostatin B. Mutant catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus
G115T
the mutant produces a five-membered ring compound as the major product with tryprostatin B as the minor product
Y205C
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
Y205F
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
Y205I
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
Y205L
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
Y205M
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
Y205S
mutant produces 50.4% C3-regularly prenylated product and 1.8% C3-reversely prenylated product
Y205S
-
significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by the mutant enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wollinsky, B.; Ludwig, L.; Hamacher, A.; Yu, X.; Kassack, M.U.; Li, S.M.
Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides
Bioorg. Med. Chem. Lett.
22
3866-3869
2012
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus Af293 (Q4WAW7)
brenda
Jost, M.; Zocher, G.; Tarcz, S.; Matuschek, M.; Xie, X.; Li, S.M.; Stehle, T.
Structure-function analysis of an enzymatic prenyl transfer reaction identifies a reaction chamber with modifiable specificity
J. Am. Chem. Soc.
132
17849-17858
2010
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus, Aspergillus fumigatus Af293 (Q4WAW7)
brenda
Zou, H.; Zheng, X.; Li, S.M.
Substrate promiscuity of the cyclic dipeptide prenyltransferases from Aspergillus fumigatus
J. Nat. Prod.
72
44-52
2009
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus Af293 (Q4WAW7)
brenda
Grundmann, A.; Li, S.M.
Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus
Microbiology
151
2199-2207
2005
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus, Aspergillus fumigatus Af293 (Q4WAW7)
brenda
Wollinsky, B.; Ludwig, L.; Xie, X.; Li, S.M.
Breaking the regioselectivity of indole prenyltransferases: identification of regular C3-prenylated hexahydropyrrolo[2,3-b]indoles as side products of the regular C2-prenyltransferase FtmPT1
Org. Biomol. Chem.
10
9262-9270
2012
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus Af293 (Q4WAW7)
brenda
Chen, J.; Morita, H.; Wakimoto, T.; Mori, T.; Noguchi, H.; Abe, I.
Prenylation of a nonaromatic carbon of indolylbutenone by a fungal indole prenyltransferase
Org. Lett.
14
3080-3083
2012
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus, Aspergillus fumigatus Af293 (Q4WAW7)
brenda
Mahmoodi, N.; Tanner, M.E.
Potential rearrangements in the reaction catalyzed by the indole prenyltransferase FtmPT1
ChemBioChem
14
2029-2037
2013
Aspergillus fumigatus
brenda
Mahmoodi, N.; Qian, Q.; Luk, L.; Tanner, M.
Rearrangements in the mechanisms of the indole alkaloid prenyltransferases
Pure Appl. Chem.
85
1935-1948
2013
Aspergillus fumigatus
-
brenda
Zhou, K.; Zhao, W.; Liu, X.; Li, S.
Saturation mutagenesis on Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 results in mutants with strongly increased C3-prenylating activity
Appl. Microbiol. Biotechnol.
100
943-9953
2016
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus ATCC MYA-4609 (Q4WAW7)
brenda
Pan, L.L.; Yang, Y.; Merz, K.M.
Origin of product selectivity in a prenyl transfer reaction from the same intermediate: exploration of multiple FtmPT1-catalyzed prenyl transfer pathways
Biochemistry
53
6126-6138
2014
Aspergillus fumigatus (Q4WAW7), Aspergillus fumigatus ATCC MYA-4609 (Q4WAW7)
brenda
Couillaud, J.; Rico, J.; Rubini, A.; Hamrouni, T.; Courvoisier-Dezord, E.; Petit, J.; Mariage, A.; Darii, E.; Duquesne, K.; De Berardinis, V.; Iacazio, G.
Simplified in vitro and in vivo bioaccess to prenylated compounds
ACS Omega
4
7838-7849
2019
Aspergillus fumigatus
-
brenda
Zhao, W.; Fan, A.; Tarcz, S.; Zhou, K.; Yin, W.B.; Liu, X.Q.; Li, S.M.
Mutation on Gly115 and Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 increases its catalytic activity toward hydroxynaphthalenes
Appl. Microbiol. Biotechnol.
101
1989-1998
2017
Aspergillus fumigatus
brenda
Pan, L.L.; Song, L.F.; Miao, Y.; Yang, Y.; Merz, K.M.
Mechanism of formation of the nonstandard product in the prenyltransferase reaction of the G115T mutant of FtmPT1 A case of reaction dynamics calling the shots?
Biochemistry
56
2995-3007
2017
Aspergillus fumigatus (Q4WAW7)
brenda
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