Any feedback?
No. of entries
Information on EC 2.5.1.109 - brevianamide F prenyltransferase (deoxybrevianamide E-forming)
for references in articles please use BRENDA:EC2.5.1.109
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.109 brevianamide F prenyltransferase (deoxybrevianamide E-forming)
IUBMB Comments
The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F , while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides . Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
The enzyme appears in viruses and cellular organisms
- 2.5.1.109
- dipeptides
-
tryptophan-containing
- aspergillus
- indole
- fischeri
- versicolor
-
proving
- synthesis
showSynonyms
brept, cyclic dipeptide c7-prenyltransferase, cdpc7pt, brevianamide f reverse prenyltransferase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BrePT
brevianamide F reverse prenyltransferase
CdpC7PT
cyclic dipeptide C7-prenyltransferase
dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-C-2-transferase
-
-
-
-
NotF
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prenyl diphosphate + brevianamide F = diphosphate + deoxybrevianamide E
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
stephacidin A biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
prenyl-diphosphate:brevianamide-F 2-methylbut-3-en-2-yl-C-2-transferase
The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F [1], while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides [2]. Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + (R)-benzodiazepinedione
diphosphate + ?
Substrates: low activity, (R)-benzodiazepinedione consists of a tryptophanyl and an anthranilyl moiety
Products: -
Products: -
?
dimethylallyl diphosphate + (S)-benzodiazepinedione
diphosphate + ?
Substrates: best substrate, (S)-benzodiazepinedione consists of a tryptophanyl and an anthranilyl moiety
Products: -
Products: -
?
dimethylallyl diphosphate + benzodiazepinedione
diphosphate + ?
Substrates: best substrate, active only with benzodiazepinedione consisting of a D-tryptophanyl and an anthranilyl moiety, poor activity with the L-Tryp isomer
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
diphosphate +
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
diphosphate + ?
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
?
Substrates: conversion yield of 6%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-D-Pro
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-D-Pro
dimethylallyl diphosphate + cyclo-D-Trp-L-Ala
?
Substrates: conversion yield of 17%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Ala
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-L-Ala
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Ala
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-L-Ala
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
?
Substrates: conversion yield of 18%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-L-Pro
Substrates: low activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-L-Pro
dimethylallyl diphosphate + cyclo-D-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-L-Trp
Substrates: low activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Ala
?
Substrates: conversion yield of 5%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Ala
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-D-Ala
Substrates: low activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Ala
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-D-Ala
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
?
Substrates: conversion yield of 61%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-D-Pro
dimethylallyl diphosphate + cyclo-L-Trp-Gly
?
Substrates: conversion yield of 6%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-Gly
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-Gly
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-Gly
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-Gly
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
?
Substrates: conversion yield of 11%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Ala
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
diphosphate + ?
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-L-Ala
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-His
?
Substrates: conversion yield of less than 3%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Leu
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Leu
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Leu
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-L-Leu
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Phe
?
Substrates: conversion yield of less than 3%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Phe
diphosphate +
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Phe
diphosphate + ?
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
?
Substrates: conversion yield of less than 3%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
?
Substrates: conversion yield of less than 3%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Tyr
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-L-Tyr
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-Xaa
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-Xaa
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Tyr-L-Tyr
diphosphate + 4-O-(3-methylbut-2-enyl)-cyclo-L-Tyr-L-Tyr
dimethylallyl diphosphate + cyclo-LTrp-L-Phe
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Phe
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
Substrates: reaction of 7-DMATS, EC 2.5.1.80, low activity
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: the enzyme is involved in the alkaloid biosynthetic pathway
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
Products: deoxybrevianamide E i.e. (3S,8aS)-3-[[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl]-octahydropyrrolo[1,2-a]piperazine-1,4-dione
Products: deoxybrevianamide E i.e. (3S,8aS)-3-[[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl]-octahydropyrrolo[1,2-a]piperazine-1,4-dione
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: i.e. cyclo-L-Trp-L-Pro, conversion yield of 66%
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: the enzyme accepts a broad range of tryptophan-containing cyclic dipeptides, no activity with farnesyl diphosphate and geranyl diphosphate
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: i.e. cyclo-L-Trp-L-Pro
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: the enzyme accepts a broad range of tryptophan-containing cyclic dipeptides, no activity with farnesyl diphosphate and geranyl diphosphate
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: the enzyme accepts a broad range of tryptophan-containing cyclic dipeptides, no activity with farnesyl diphosphate and geranyl diphosphate
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
?
Substrates: conversion yield of 1%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
?
Substrates: conversion yield of less than 3%
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-D-Pro
Substrates: low activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-L-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-L-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-L-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-D-Pro
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
Substrates: attachment of the prenyl moiety to C-7 of the indole ring
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
Substrates: higher activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
Substrates: attachment of the prenyl moiety to C-7 of the indole ring
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Tyr
Substrates: higher activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Tyr
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Tyr
Substrates: higher activity
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Tyr-L-Tyr
diphosphate + 4-O-(3-methylbut-2-enyl)-cyclo-L-Tyr-L-Tyr
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Tyr-L-Tyr
diphosphate + 4-O-(3-methylbut-2-enyl)-cyclo-L-Tyr-L-Tyr
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses cyclic dipeptides containing L-Trp and attaches the prenyl moiety to C-7 of the indole ring. The enzyme showsma relatively narrow substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows no activity with L-Trp, cyclo-L-Trp-L-Trp, cyclo-L-Phe-L-Pro and cyclo-L-Trp-L-Tyr
Products: -
Products: -
?
additional information
?
-
Substrates: for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
Products: -
Products: -
?
additional information
?
-
-
Substrates: for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme uses cyclic dipeptides containing L-Trp and attaches the prenyl moiety to C-7 of the indole ring. It also accepts cyclo-L-Tyr-L-Tyr as substrate and catalyzes an O-prenylation at the tyrosyl residue of the dipeptide cyclo-L-Trp-L-Tyr. Substrate specificity, overview. Cyclo-L-Tyr-L-Ser, cyclo-L-Tyr-L-Pro, cyclo-L-Tyr-Gly, and L-tyrosine are poor substrates. CdpC7PT shows a high affinity to its prenyl donor dimethylallyl diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses cyclic dipeptides containing L-Trp and attaches the prenyl moiety to C-7 of the indole ring. It also accepts cyclo-L-Tyr-L-Tyr as substrate and catalyzes an O-prenylation at the tyrosyl residue of the dipeptide cyclo-L-Trp-L-Tyr. Substrate specificity, overview. Cyclo-L-Tyr-L-Ser, cyclo-L-Tyr-L-Pro, cyclo-L-Tyr-Gly, and L-tyrosine are poor substrates. CdpC7PT shows a high affinity to its prenyl donor dimethylallyl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme uses cyclic dipeptides containing L-Trp and attaches the prenyl moiety to C-7 of the indole ring, no activity with cyclo-L-Trp-L-Pro, cyclo-L-Trp-D-Pro, cyclo-D-Trp-L-Pro, cyclo-D-Trp-D-Pro, and cyclo-L-Trp-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses cyclic dipeptides containing L-Trp and attaches the prenyl moiety to C-7 of the indole ring, no activity with cyclo-L-Trp-L-Pro, cyclo-L-Trp-D-Pro, cyclo-D-Trp-L-Pro, cyclo-D-Trp-D-Pro, and cyclo-L-Trp-Gly
Products: -
Products: -
?
additional information
?
-
Substrates: for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme uses cyclic dipeptides containing L-Trp and attaches the prenyl moiety to C-7 of the indole ring. It also accepts cyclo-L-Tyr-L-Tyr as substrate and catalyzes an O-prenylation at the tyrosyl residue of the dipeptide cyclo-L-Trp-L-Tyr. Substrate specificity, overview. Cyclo-L-Tyr-L-Ser, cyclo-L-Tyr-L-Pro, cyclo-L-Tyr-Gly, and L-tyrosine are poor substrates. CdpC7PT shows a high affinity to its prenyl donor dimethylallyl diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows high flexibility towards its aromatic substrates and accepts all of the 14 tested tryptophan-containing cyclic dipeptides. The enzyme catalyzes the highly regiospecific reverse prenylation at C2 of the indole nucleus
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows high flexibility towards its aromatic substrates and accepts all of the 14 tested tryptophan-containing cyclic dipeptides. The enzyme catalyzes the highly regiospecific reverse prenylation at C2 of the indole nucleus
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
dimethylallyl diphosphate + cyclo-L-Trp-Xaa
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-Xaa
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: the enzyme is involved in the alkaloid biosynthetic pathway
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
Substrates: attachment of the prenyl moiety to C-7 of the indole ring
Products: -
Products: -
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
Substrates: attachment of the prenyl moiety to C-7 of the indole ring
Products: -
Products: -
?
additional information
?
-
Substrates: for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
Products: -
Products: -
?
additional information
?
-
-
Substrates: for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
Products: -
Products: -
?
additional information
?
-
Substrates: for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
additional information
Ca2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Mg2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Mn2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
additional information
no significant effect by 5 mM EDTA. The enzyme reaction of CdpC7PT is independent of metal ions, but can be enhanced by Ca2+, Mn2+, and Mg2+
additional information
-
no significant effect by 5 mM EDTA. The enzyme reaction of CdpC7PT is independent of metal ions, but can be enhanced by Ca2+, Mn2+, and Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics, for the tryptophan-containing cyclic dipeptides, KM values between 0.239 and 0.747 mM and turnover numbers in the range of 0.009-0.049/s are determined
-
additional information
additional information
-
Michaelis-Menten kinetics, for the tryptophan-containing cyclic dipeptides, KM values between 0.239 and 0.747 mM and turnover numbers in the range of 0.009-0.049/s are determined
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
pH 5.0: about 50% of maximal activity, pH 10.0: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
the enzyme is involved in the biosynthesis of notoamides
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). NOTF_ASPSM
Aspergillus sp. (strain MF297-2)
452
0
51608
Swiss-Prot
other Location (Reliability: 3)
Q0CQ16_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
446
0
50990
TrEMBL
Secretory Pathway (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ATEG_04218 or cdpC7PT, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain M15
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
regularly C7-prenylated cyclic dipeptides are successfully obtained by using the member of the DMATS family, CdpC7PT from Aspergillus terreus
synthesis
-
regularly C7-prenylated cyclic dipeptides are successfully obtained by using the member of the DMATS family, CdpC7PT from Aspergillus terreus
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yin, S.; Yu, X.; Wang, Q.; Liu, X.Q.; Li, S.M.
Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides
Appl. Microbiol. Biotechnol.
97
1649-1660
2013
Aspergillus versicolor (I4AY86), Aspergillus versicolor, Aspergillus versicolor NRRL 573 (I4AY86), Aspergillus versicolor NRRL573 (I4AY86), Aspergillus versicolor NRRL573
brenda
Ding, Y.; de Wet, J.R.; Cavalcoli, J.; Li, S.; Greshock, T.J.; Miller, K.A.; Finefield, J.M.; Sunderhaus, J.D.; McAfoos, T.J.; Tsukamoto, S.; Williams, R.M.; Sherman, D.H.
Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp.
J. Am. Chem. Soc.
132
12733-12740
2010
Aspergillus sp. (E0Y3X1)
brenda
Wunsch, C.; Zou, H.X.; Linne, U.; Li, S.M.
C7-prenylation of tryptophanyl and O-prenylation of tyrosyl residues in dipeptides by an Aspergillus terreus prenyltransferase
Appl. Microbiol. Biotechnol.
99
1719-1730
2015
Aspergillus oryzae, Aspergillus terreus (Q0CQ16), Aspergillus terreus, Aspergillus terreus DSM 1958 (Q0CQ16)
brenda
Yang, K.; Li, S.M.; Liu, X.; Fan, A.
Reinvestigation of the substrate specificity of a reverse prenyltransferase NotF from Aspergillus sp. MF297-2
Arch. Microbiol.
202
1419-1424
2020
Aspergillus sp. MF297-2 (E0Y3X1)
brenda
EXTERNAL LINKS (specific for EC-Number 2.5.1.109)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
