BRENDA - Enzyme Database show
show all sequences of 2.5.1.109

Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp.

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.; J. Am. Chem. Soc. 132, 12733-12740 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Aspergillus sp.
Engineering
Amino acid exchange
Commentary
Organism
E108D
mutant loses at least 92% of its activity
Aspergillus sp.
E108G
mutant loses at least 92% of its activity
Aspergillus sp.
R122G
mutant with less than 2% catalytic activity
Aspergillus sp.
R122H
mutant with less than 2% catalytic activity
Aspergillus sp.
W424G
mutant loses more than 98% of its activity
Aspergillus sp.
W424Y
mutant retains about 25% of its activity
Aspergillus sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
5 mM, about 90% loss of activity
Aspergillus sp.
Fe2+
5 mM, about 65% loss of activity
Aspergillus sp.
Sn2+
5 mM, about 90% loss of activity
Aspergillus sp.
Zn2+
5 mM, about 90% loss of activity
Aspergillus sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00131
-
dimethylallyl diphosphate
pH 7.5, 22°C
Aspergillus sp.
0.00433
-
brevianamide F
pH 7.5, 22°C
Aspergillus sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Aspergillus sp.
Mg2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Aspergillus sp.
Mn2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Aspergillus sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53600
-
x * 53600, calculated from sequence
Aspergillus sp.
292000
-
gel filtration
Aspergillus sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dimethylallyl diphosphate + brevianamide F
Aspergillus sp.
the enzyme is involved in the alkaloid biosynthetic pathway
diphosphate + deoxybrevianamide E
-
-
?
dimethylallyl diphosphate + brevianamide F
Aspergillus sp. MF297-2
the enzyme is involved in the alkaloid biosynthetic pathway
diphosphate + deoxybrevianamide E
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus sp.
E0Y3X1
-
-
Aspergillus sp. MF297-2
E0Y3X1
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dimethylallyl diphosphate + brevianamide F
the enzyme is involved in the alkaloid biosynthetic pathway
722446
Aspergillus sp.
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
722446
Aspergillus sp.
diphosphate + deoxybrevianamide E
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
the enzyme is involved in the alkaloid biosynthetic pathway
722446
Aspergillus sp. MF297-2
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
722446
Aspergillus sp. MF297-2
diphosphate + deoxybrevianamide E
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
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 53600, calculated from sequence
Aspergillus sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
40
-
Aspergillus sp.
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
50
20-40: maximal activity, 50°C: about 30% of maximal activity
Aspergillus sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.32
-
brevianamide F
pH 7.5, 22°C
Aspergillus sp.
0.42
-
dimethylallyl diphosphate
pH 7.5, 22°C
Aspergillus sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
9
-
Aspergillus sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
10
pH 5.0: about 50% of maximal activity, pH 10.0: about 70% of maximal activity
Aspergillus sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Aspergillus sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E108D
mutant loses at least 92% of its activity
Aspergillus sp.
E108G
mutant loses at least 92% of its activity
Aspergillus sp.
R122G
mutant with less than 2% catalytic activity
Aspergillus sp.
R122H
mutant with less than 2% catalytic activity
Aspergillus sp.
W424G
mutant loses more than 98% of its activity
Aspergillus sp.
W424Y
mutant retains about 25% of its activity
Aspergillus sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
5 mM, about 90% loss of activity
Aspergillus sp.
Fe2+
5 mM, about 65% loss of activity
Aspergillus sp.
Sn2+
5 mM, about 90% loss of activity
Aspergillus sp.
Zn2+
5 mM, about 90% loss of activity
Aspergillus sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00131
-
dimethylallyl diphosphate
pH 7.5, 22°C
Aspergillus sp.
0.00433
-
brevianamide F
pH 7.5, 22°C
Aspergillus sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Aspergillus sp.
Mg2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Aspergillus sp.
Mn2+
enzyme activity is independent of divalent cation, although addition of 5 mM Mg2+, Ca2+ or Mn2+ slightly enhances catalysis (about 100-120%)
Aspergillus sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53600
-
x * 53600, calculated from sequence
Aspergillus sp.
292000
-
gel filtration
Aspergillus sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dimethylallyl diphosphate + brevianamide F
Aspergillus sp.
the enzyme is involved in the alkaloid biosynthetic pathway
diphosphate + deoxybrevianamide E
-
-
?
dimethylallyl diphosphate + brevianamide F
Aspergillus sp. MF297-2
the enzyme is involved in the alkaloid biosynthetic pathway
diphosphate + deoxybrevianamide E
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dimethylallyl diphosphate + brevianamide F
the enzyme is involved in the alkaloid biosynthetic pathway
722446
Aspergillus sp.
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
722446
Aspergillus sp.
diphosphate + deoxybrevianamide E
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
the enzyme is involved in the alkaloid biosynthetic pathway
722446
Aspergillus sp. MF297-2
diphosphate + deoxybrevianamide E
-
-
-
?
dimethylallyl diphosphate + brevianamide F
the enzyme is specific for brevianamide F i.e. (3S,8aS)-3-(1H-indol-3-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
722446
Aspergillus sp. MF297-2
diphosphate + deoxybrevianamide E
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
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 53600, calculated from sequence
Aspergillus sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
40
-
Aspergillus sp.
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
50
20-40: maximal activity, 50°C: about 30% of maximal activity
Aspergillus sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.32
-
brevianamide F
pH 7.5, 22°C
Aspergillus sp.
0.42
-
dimethylallyl diphosphate
pH 7.5, 22°C
Aspergillus sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
9
-
Aspergillus sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
10
pH 5.0: about 50% of maximal activity, pH 10.0: about 70% of maximal activity
Aspergillus sp.
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
73
-
brevianamide F
pH 7.5, 22°C
Aspergillus sp.
320
-
dimethylallyl diphosphate
pH 7.5, 22°C
Aspergillus sp.
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
73
-
brevianamide F
pH 7.5, 22°C
Aspergillus sp.
320
-
dimethylallyl diphosphate
pH 7.5, 22°C
Aspergillus sp.
Other publictions for EC 2.5.1.109
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737541
Wunsch
C7-prenylation of tryptophanyl ...
Aspergillus oryzae, Aspergillus terreus, Aspergillus terreus DSM 1958
Appl. Microbiol. Biotechnol.
99
1719-1730
2015
-
1
1
-
-
-
-
4
-
4
1
4
-
6
-
-
1
-
-
2
-
-
32
-
1
-
-
3
1
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
4
-
4
1
4
-
-
-
1
-
2
-
-
32
-
1
-
-
3
1
-
-
-
-
2
2
-
-
-
721391
Yin
Identification of a brevianami ...
Aspergillus versicolor, Aspergillus versicolor NRRL 573, Aspergillus versicolor NRRL573
Appl. Microbiol. Biotechnol.
97
1649-1660
2013
-
-
1
-
-
-
-
14
-
-
1
3
-
7
-
-
1
-
-
-
-
-
36
1
-
-
-
14
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
14
-
-
1
3
-
-
-
1
-
-
-
-
36
1
-
-
-
14
-
-
-
-
-
-
-
-
15
15
722446
Ding
Genome-based characterization ...
Aspergillus sp., Aspergillus sp. MF297-2
J. Am. Chem. Soc.
132
12733-12740
2010
-
-
1
-
6
-
4
2
-
3
2
2
-
2
-
-
-
-
-
-
-
-
4
1
1
1
-
2
1
1
-
-
-
-
-
-
-
1
-
-
6
-
-
4
-
2
-
3
2
2
-
-
-
-
-
-
-
-
4
1
1
1
-
2
1
1
-
-
-
-
-
-
2
2