BRENDA - Enzyme Database show
show all sequences of 2.5.1.122

A new member of the DMATS superfamily from Aspergillus niger catalyzes prenylations of both tyrosine and tryptophan derivatives

Fan, A.; Chen, H.; Wu, R.; Xu, H.; Li, S.M.; Appl. Microbiol. Biotechnol. 98, 10119-10129 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene An13g01840, DNA and amino acid sequence determination and analysis, overexpression of His6-tagged enzyme in Escherichia coli strain SoluBL21, subcloning in Escherichia coli strain XL1 BlueMRF'
Aspergillus niger
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
strong inhibition
Aspergillus niger
Zn2+
slight inhibition
Aspergillus niger
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.19
-
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37°C
Aspergillus niger
0.19
-
L-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.22
-
D-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.24
-
L-tyrosine
at pH 7.5 and 37°C; pH 7.5, 37°C
Aspergillus niger
0.25
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.29
-
3-iodo-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.42
-
alpha-Methyl-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.69
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.71
-
dimethylallyl diphosphate
pH 7.5, 37°C; with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C
Aspergillus niger
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Aspergillus niger
Mg2+
activates
Aspergillus niger
additional information
addition of K+, Na+, Mg2+, Mn2+, Co2+, or EDTA to the reaction mixture does not change the enzyme activity significantly; no significant effects on enzyme activity by K+, Na+, Mg2+, Mn2+, Co2+, or EDTA
Aspergillus niger
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52700
-
; x * 52700, calculated from amino acid sequence
Aspergillus niger
53500
-
-
Aspergillus niger
228000
-
recombinant His6-tagged enzyme, gel filtration
Aspergillus niger
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dimethylallyl diphosphate + L-tyrosine
Aspergillus niger
-
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus niger
A2R1N3
gene An13g01840 or ANI_1_660114
-
Aspergillus niger
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21 to near homogeneity by nickel affinity chromatography and desalting gel filtration
Aspergillus niger
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus niger
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
98% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
-
729072
Aspergillus niger
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
53% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
100% activity
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
-
729072
Aspergillus niger
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
23% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
prenylation at 4-O- or N-atom
729072
Aspergillus niger
diphosphate + 4-dimethylallylamino-L-phenylalanine
-
-
-
?
dimethylallyl diphosphate + 4-methyl-DL-tryptophan
13% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 4-methyl-DL-tryptophan
41% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 7-dimethylallyl-4-methyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + 5-methyl-DL-tryptophan
10% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 7-dimethylally-5-methyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + alpha-methyl-L-tyrosine
98% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + D-tyrosine
33% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + D-tyrosine
-
729072
Aspergillus niger
diphosphate + 4-O-dimethylallyl-D-tyrosine
-
-
-
?
dimethylallyl diphosphate + L-tryptophan
33% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 7-dimethylallyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
-
729072
Aspergillus niger
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
98% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
?
additional information
the enzyme shows a wider substrate spectrum compared to tyrosine prenyltransferase SirD. It catalyzes O-prenylation of L-tyrosine, EC 2.5.1.122, and also accepts 4-amino-L-phenylalanine for an N-prenylation and L-tryptophan for a C7-prenylation, EC 2.5.1.80. It is also active with 4-amino-L-phenylalanine as well as 4- and 5-methyl-DL-tryptophan. HRMS analysis of the enzyme products, overview. 3,5-dibromo-L-tyrosine is a poor substrate
729072
Aspergillus niger
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 52700, calculated from amino acid sequence; x * 53500, recombinant His6-tagged enzyme, SDS-PAGE, x * 52700, about, sequence calculation
Aspergillus niger
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Aspergillus niger
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0036
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.0053
-
L-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.16
-
3-iodo-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.16
-
D-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.2
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.26
-
alpha-Methyl-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.27
-
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37°C
Aspergillus niger
0.58
-
L-tyrosine
at pH 7.5 and 37°C; pH 7.5, 37°C
Aspergillus niger
0.69
-
dimethylallyl diphosphate
with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C
Aspergillus niger
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Aspergillus niger
Cloned(Commentary) (protein specific)
Commentary
Organism
gene An13g01840, DNA and amino acid sequence determination and analysis, overexpression of His6-tagged enzyme in Escherichia coli strain SoluBL21, subcloning in Escherichia coli strain XL1 BlueMRF'
Aspergillus niger
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
strong inhibition
Aspergillus niger
Zn2+
slight inhibition
Aspergillus niger
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.19
-
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37°C
Aspergillus niger
0.19
-
L-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.22
-
D-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.24
-
L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.24
-
L-tyrosine
pH 7.5, 37°C
Aspergillus niger
0.25
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.29
-
3-iodo-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.42
-
alpha-Methyl-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.69
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.71
-
dimethylallyl diphosphate
with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C
Aspergillus niger
0.71
-
dimethylallyl diphosphate
pH 7.5, 37°C
Aspergillus niger
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Aspergillus niger
Mg2+
activates
Aspergillus niger
additional information
addition of K+, Na+, Mg2+, Mn2+, Co2+, or EDTA to the reaction mixture does not change the enzyme activity significantly
Aspergillus niger
additional information
no significant effects on enzyme activity by K+, Na+, Mg2+, Mn2+, Co2+, or EDTA
Aspergillus niger
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52700
-
x * 52700, calculated from amino acid sequence
Aspergillus niger
52700
-
-
Aspergillus niger
53500
-
-
Aspergillus niger
228000
-
recombinant His6-tagged enzyme, gel filtration
Aspergillus niger
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dimethylallyl diphosphate + L-tyrosine
Aspergillus niger
-
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21 to near homogeneity by nickel affinity chromatography and desalting gel filtration
Aspergillus niger
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus niger
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
98% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 3,4-dihydroxy-L-phenylalanine
-
729072
Aspergillus niger
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + 3-fluoro-DL-tyrosine
53% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
100% activity
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 3-iodo-L-tyrosine
-
729072
Aspergillus niger
diphosphate + ?
-
-
-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
23% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 4-amino-L-phenylalanine
prenylation at 4-O- or N-atom
729072
Aspergillus niger
diphosphate + 4-dimethylallylamino-L-phenylalanine
-
-
-
?
dimethylallyl diphosphate + 4-methyl-DL-tryptophan
13% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + 4-methyl-DL-tryptophan
41% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 7-dimethylallyl-4-methyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + 5-methyl-DL-tryptophan
10% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 7-dimethylally-5-methyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + alpha-methyl-L-tyrosine
98% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + D-tyrosine
33% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
?
-
-
-
?
dimethylallyl diphosphate + D-tyrosine
-
729072
Aspergillus niger
diphosphate + 4-O-dimethylallyl-D-tyrosine
-
-
-
?
dimethylallyl diphosphate + L-tryptophan
33% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 7-dimethylallyl-L-tryptophan
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
-
729072
Aspergillus niger
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
?
dimethylallyl diphosphate + L-tyrosine
98% activity compared to 3-iodo-L-tyrosine
729072
Aspergillus niger
diphosphate + 4-O-dimethylallyl-L-tyrosine
-
-
-
?
additional information
the enzyme shows a wider substrate spectrum compared to tyrosine prenyltransferase SirD. It catalyzes O-prenylation of L-tyrosine, EC 2.5.1.122, and also accepts 4-amino-L-phenylalanine for an N-prenylation and L-tryptophan for a C7-prenylation, EC 2.5.1.80. It is also active with 4-amino-L-phenylalanine as well as 4- and 5-methyl-DL-tryptophan. HRMS analysis of the enzyme products, overview. 3,5-dibromo-L-tyrosine is a poor substrate
729072
Aspergillus niger
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 52700, calculated from amino acid sequence
Aspergillus niger
?
x * 53500, recombinant His6-tagged enzyme, SDS-PAGE, x * 52700, about, sequence calculation
Aspergillus niger
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Aspergillus niger
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0036
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.0053
-
L-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.16
-
3-iodo-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.16
-
D-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.2
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.26
-
alpha-Methyl-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.27
-
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37°C
Aspergillus niger
0.58
-
L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.58
-
L-tyrosine
pH 7.5, 37°C
Aspergillus niger
0.69
-
dimethylallyl diphosphate
with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C
Aspergillus niger
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Aspergillus niger
General Information
General Information
Commentary
Organism
evolution
the enzyme is a member of the DMATS superfamily
Aspergillus niger
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme is a member of the DMATS superfamily
Aspergillus niger
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.028
-
L-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.043
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.551
-
3-iodo-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.619
-
alpha-Methyl-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.727
-
D-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.8
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.972
-
dimethylallyl diphosphate
with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C
Aspergillus niger
1.421
-
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37°C
Aspergillus niger
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.028
-
L-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.043
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.551
-
3-iodo-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.619
-
alpha-Methyl-L-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.727
-
D-tyrosine
at pH 7.5 and 37°C
Aspergillus niger
0.8
-
4-methyl-DL-tryptophan
at pH 7.5 and 37°C
Aspergillus niger
0.972
-
dimethylallyl diphosphate
with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C
Aspergillus niger
1.421
-
3,4-dihydroxy-L-phenylalanine
at pH 7.5 and 37°C
Aspergillus niger
Other publictions for EC 2.5.1.122
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)
737543
Yu
Tyrosine O-prenyltransferases ...
Aspergillus niger, Leptosphaeria maculans
Appl. Microbiol. Biotechnol.
99
7115-7124
2015
-
-
-
-
-
-
-
8
-
-
-
-
-
4
-
-
-
-
-
-
-
-
32
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
32
-
-
-
-
8
-
-
-
-
-
-
-
-
7
7
738647
Fan
Site-directed mutagenesis swit ...
Aspergillus fumigatus
J. Biol. Chem.
290
1364-1373
2015
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739221
Fan
Tryptophan prenyltransferases ...
Aspergillus niger
Org. Biomol. Chem.
13
7551-7557
2015
-
-
-
-
-
-
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
-
4
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
4
-
1
-
-
1
1
-
-
-
-
1
1
-
1
1
729072
Fan
A new member of the DMATS supe ...
Aspergillus niger
Appl. Microbiol. Biotechnol.
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