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Information on EC 2.5.1.109 - brevianamide F prenyltransferase (deoxybrevianamide E-forming)
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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.
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Word Map
- 2.5.1.109
- dipeptides
-
tryptophan-containing
- aspergillus
- indole
- fischeri
- versicolor
-
proving
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
brept, cyclic dipeptide c7-prenyltransferase, cdpc7pt, brevianamide f reverse prenyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BrePT
brevianamide F reverse prenyltransferase
CdpC7PT
cyclic dipeptide C7-prenyltransferase
NotF
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + brevianamide F = diphosphate + deoxybrevianamide E
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:brevianamide-F tert-dimethylallyl-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.
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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
dimethylallyl diphosphate + (R)-benzodiazepinedione
diphosphate + ?
low activity, (R)-benzodiazepinedione consists of a tryptophanyl and an anthranilyl moiety
-
-
?
dimethylallyl diphosphate + (S)-benzodiazepinedione
diphosphate + ?
best substrate, (S)-benzodiazepinedione consists of a tryptophanyl and an anthranilyl moiety
-
-
?
dimethylallyl diphosphate + benzodiazepinedione
diphosphate + ?
best substrate, active only with benzodiazepinedione consisting of a D-tryptophanyl and an anthranilyl moiety, poor activity with the L-Tryp isomer
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Pro
?
conversion yield of 6%
-
-
?
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
?
conversion yield of 17%
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Ala
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-L-Ala
-
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Ala
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-D-Trp]-L-Ala
-
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
?
conversion yield of 18%
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-L-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-L-Pro
low activity
-
-
?
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
low activity
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Ala
?
conversion yield of 5%
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Ala
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-D-Ala
low activity
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Ala
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-D-Ala
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
?
conversion yield of 61%
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-D-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-D-Pro
-
-
-
?
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
?
conversion yield of 6%
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-Gly
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-Gly
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-Gly
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-Gly
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
?
conversion yield of 11%
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Ala
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Ala
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-L-Ala
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-His
?
conversion yield of less than 3%
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Leu
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Leu
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Leu
diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-L-Leu
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Phe
?
conversion yield of less than 3%
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Phe
diphosphate +
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Phe
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Pro
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Pro
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
?
conversion yield of less than 3%
-
-
?
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
?
conversion yield of less than 3%
-
-
?
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
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-Xaa
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-Xaa
-
-
-
-
?
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
-
-
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
the enzyme is involved in the alkaloid biosynthetic pathway
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
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
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
i.e. cyclo-L-Trp-L-Pro, conversion yield of 66%
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
the enzyme accepts a broad range of tryptophan-containing cyclic dipeptides, no activity with farnesyl diphosphate and geranyl diphosphate
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
i.e. cyclo-L-Trp-L-Pro
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
the enzyme accepts a broad range of tryptophan-containing cyclic dipeptides, no activity with farnesyl diphosphate and geranyl diphosphate
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
i.e. cyclo-L-Trp-L-Pro
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
the enzyme accepts a broad range of tryptophan-containing cyclic dipeptides, no activity with farnesyl diphosphate and geranyl diphosphate
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
i.e. cyclo-L-Trp-L-Pro
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
?
conversion yield of 1%
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
?
conversion yield of less than 3%
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
diphosphate +
-
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
diphosphate +
-
-
-
?
dimethylallyl diphosphate + cyclo-D-Trp-D-Ala
diphosphate +
-
-
-
?
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 + 7-(3-methylbut-2-enyl)-cyclo-D-Trp-D-Pro
low activity
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
higher activity
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
attachment of the prenyl moiety to C-7 of the indole ring
-
-
?
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
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Tyr
-
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-L-Tyr
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Tyr
higher activity
-
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
reaction of 7-DMATS, EC 2.5.1.80, low activity
-
-
?
dimethylallyl diphosphate + L-tryptophan
diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
reaction of 7-DMATS, EC 2.5.1.80, low activity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme shows no activity with L-Trp, cyclo-L-Trp-L-Trp, cyclo-L-Phe-L-Pro and cyclo-L-Trp-L-Tyr
-
-
-
additional information
?
-
for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
-
-
?
additional information
?
-
-
for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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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
dimethylallyl diphosphate + cyclo-L-Trp-L-Trp
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Trp
attachment of the prenyl moiety to C-7 of the indole ring
-
-
?
dimethylallyl diphosphate + cyclo-L-Trp-Xaa
diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-Xaa
-
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
the enzyme is involved in the alkaloid biosynthetic pathway
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
diphosphate + deoxybrevianamide E
-
-
-
?
additional information
?
-
for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
-
-
?
additional information
?
-
-
for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
-
-
?
additional information
?
-
for some substrates, reversely C3- or N1-prenylated derivatives are identified as minor products
-
-
?
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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+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
pH 5.0: about 50% of maximal activity, pH 10.0: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
the enzyme is involved in the biosynthesis of notoamides
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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). NOTF_ASPSM
Aspergillus sp. (strain MF297-2)
452
0
51608
Swiss-Prot
other Location (Reliability: 1)
NOTF_ASPVE
435
0
49567
Swiss-Prot
other Location (Reliability: 5)
Q0CQ16_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
446
0
50990
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography
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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
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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
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regularly C7-prenylated cyclic dipeptides are successfully obtained by using the member of the DMATS family, CdpC7PT from Aspergillus terreus
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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
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Release 2023.1 (January 2023)
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