BRENDA - Enzyme Database
show all sequences of 1.1.99.29

Simple and efficient expression of Agaricus meleagris pyranose dehydrogenase in Pichia pastoris

Sygmund, C.; Gutmann, A.; Krondorfer, I.; Kujawa, M.; Glieder, A.; Pscheidt, B.; Haltrich, D.; Peterbauer, C.; Kittl, R.; Appl. Microbiol. Biotechnol. 94, 695-704 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Pichia pastoris strain CBS 7435
Leucoagaricus meleagris
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.13
-
ferrocenium ion
native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.16
-
ferrocenium ion
recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.49
-
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.54
-
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.55
-
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
0.62
-
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
0.69
-
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.82
-
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.05
-
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.07
-
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.38
-
1,4-benzoquinone
recombinant enzyme, at pH 4.0 and 30°C
Leucoagaricus meleagris
1.82
-
1,4-benzoquinone
native enzyme, at pH 3.0 and 30°C
Leucoagaricus meleagris
1.92
-
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.93
-
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
128
-
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
134
-
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61967
-
x * 61967, calculated from amino acid sequence
Leucoagaricus meleagris
64000
-
x * 64000, deglycosylated protein, SDS-PAGE
Leucoagaricus meleagris
93000
-
x * 93000, recombinant enzyme, SDS-PAGE
Leucoagaricus meleagris
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-galactose + ferrocenium ion
Leucoagaricus meleagris
-
2-dehydro-D-galactose + ferrocene
-
-
?
D-glucose + 1,4-benzoquinone
Leucoagaricus meleagris
-
?
-
-
?
D-glucose + 2-chloro-1,4-benzoquinone
Leucoagaricus meleagris
-
?
-
-
?
D-glucose + ferrocenium ion
Leucoagaricus meleagris
-
3-dehydro-D-glucose + ferrocene
-
-
?
D-xylose + ferrocenium ion
Leucoagaricus meleagris
-
? + ferrocene
-
-
?
L-arabinose + ferrocenium ion
Leucoagaricus meleagris
-
? + ferrocene
-
-
?
lactose + ferrocenium ion
Leucoagaricus meleagris
-
? + ferrocene
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leucoagaricus meleagris
Q3L245
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
the level of glycosylation of recombinant enzyme is approximately 30%
Leucoagaricus meleagris
Purification (Commentary)
Commentary
Organism
DEAE Sepharose column chromatography and phenyl Sepharose column chromatography
Leucoagaricus meleagris
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
11.5
-
culture supernatant, at pH 8.5 and 30°C
Leucoagaricus meleagris
21.9
-
after 1.9fold purification, at pH 8.5 and 30°C
Leucoagaricus meleagris
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + ferrocenium ion
-
724070
Leucoagaricus meleagris
2-dehydro-D-galactose + ferrocene
-
-
-
?
D-glucose + 1,4-benzoquinone
-
724070
Leucoagaricus meleagris
?
-
-
-
?
D-glucose + 2-chloro-1,4-benzoquinone
-
724070
Leucoagaricus meleagris
?
-
-
-
?
D-glucose + ferrocenium ion
-
724070
Leucoagaricus meleagris
3-dehydro-D-glucose + ferrocene
-
-
-
?
D-xylose + ferrocenium ion
-
724070
Leucoagaricus meleagris
? + ferrocene
-
-
-
?
L-arabinose + ferrocenium ion
-
724070
Leucoagaricus meleagris
? + ferrocene
-
-
-
?
lactose + ferrocenium ion
-
724070
Leucoagaricus meleagris
? + ferrocene
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 61967, calculated from amino acid sequence; x * 64000, deglycosylated protein, SDS-PAGE; x * 93000, recombinant enzyme, SDS-PAGE
Leucoagaricus meleagris
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
12.9
-
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
15.1
-
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
34.7
-
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
37.2
-
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
37.8
-
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
39.6
-
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
41
-
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
43.4
-
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
45.9
-
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
47.3
-
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
48.5
-
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
62.4
-
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
65.4
-
1,4-benzoquinone
recombinant enzyme, at pH 4.0 and 30°C
Leucoagaricus meleagris
76
-
1,4-benzoquinone
native enzyme, at pH 3.0 and 30°C
Leucoagaricus meleagris
104
-
ferrocenium ion
native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
130
-
ferrocenium ion
recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
Cofactor
Cofactor
Commentary
Organism
Structure
flavin
-
Leucoagaricus meleagris
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Pichia pastoris strain CBS 7435
Leucoagaricus meleagris
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
flavin
-
Leucoagaricus meleagris
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.13
-
ferrocenium ion
native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.16
-
ferrocenium ion
recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.49
-
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.54
-
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.55
-
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
0.62
-
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
0.69
-
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.82
-
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.05
-
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.07
-
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.38
-
1,4-benzoquinone
recombinant enzyme, at pH 4.0 and 30°C
Leucoagaricus meleagris
1.82
-
1,4-benzoquinone
native enzyme, at pH 3.0 and 30°C
Leucoagaricus meleagris
1.92
-
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
1.93
-
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
128
-
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
134
-
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
61967
-
x * 61967, calculated from amino acid sequence
Leucoagaricus meleagris
64000
-
x * 64000, deglycosylated protein, SDS-PAGE
Leucoagaricus meleagris
93000
-
x * 93000, recombinant enzyme, SDS-PAGE
Leucoagaricus meleagris
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-galactose + ferrocenium ion
Leucoagaricus meleagris
-
2-dehydro-D-galactose + ferrocene
-
-
?
D-glucose + 1,4-benzoquinone
Leucoagaricus meleagris
-
?
-
-
?
D-glucose + 2-chloro-1,4-benzoquinone
Leucoagaricus meleagris
-
?
-
-
?
D-glucose + ferrocenium ion
Leucoagaricus meleagris
-
3-dehydro-D-glucose + ferrocene
-
-
?
D-xylose + ferrocenium ion
Leucoagaricus meleagris
-
? + ferrocene
-
-
?
L-arabinose + ferrocenium ion
Leucoagaricus meleagris
-
? + ferrocene
-
-
?
lactose + ferrocenium ion
Leucoagaricus meleagris
-
? + ferrocene
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
the level of glycosylation of recombinant enzyme is approximately 30%
Leucoagaricus meleagris
Purification (Commentary) (protein specific)
Commentary
Organism
DEAE Sepharose column chromatography and phenyl Sepharose column chromatography
Leucoagaricus meleagris
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
11.5
-
culture supernatant, at pH 8.5 and 30°C
Leucoagaricus meleagris
21.9
-
after 1.9fold purification, at pH 8.5 and 30°C
Leucoagaricus meleagris
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + ferrocenium ion
-
724070
Leucoagaricus meleagris
2-dehydro-D-galactose + ferrocene
-
-
-
?
D-glucose + 1,4-benzoquinone
-
724070
Leucoagaricus meleagris
?
-
-
-
?
D-glucose + 2-chloro-1,4-benzoquinone
-
724070
Leucoagaricus meleagris
?
-
-
-
?
D-glucose + ferrocenium ion
-
724070
Leucoagaricus meleagris
3-dehydro-D-glucose + ferrocene
-
-
-
?
D-xylose + ferrocenium ion
-
724070
Leucoagaricus meleagris
? + ferrocene
-
-
-
?
L-arabinose + ferrocenium ion
-
724070
Leucoagaricus meleagris
? + ferrocene
-
-
-
?
lactose + ferrocenium ion
-
724070
Leucoagaricus meleagris
? + ferrocene
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 61967, calculated from amino acid sequence; x * 64000, deglycosylated protein, SDS-PAGE; x * 93000, recombinant enzyme, SDS-PAGE
Leucoagaricus meleagris
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
12.9
-
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
15.1
-
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
34.7
-
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
37.2
-
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
37.8
-
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
39.6
-
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
41
-
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
43.4
-
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
45.9
-
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
47.3
-
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
48.5
-
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
62.4
-
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
65.4
-
1,4-benzoquinone
recombinant enzyme, at pH 4.0 and 30°C
Leucoagaricus meleagris
76
-
1,4-benzoquinone
native enzyme, at pH 3.0 and 30°C
Leucoagaricus meleagris
104
-
ferrocenium ion
native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
130
-
ferrocenium ion
recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.29
-
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.32
-
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
20.9
-
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
22.9
-
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
25.5
-
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
32.5
-
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
44.2
-
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
46.2
-
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
54.4
-
1,4-benzoquinone
recombinant enzyme, at pH 4.0 and 30°C
Leucoagaricus meleagris
54.8
-
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
57.5
-
1,4-benzoquinone
native enzyme, at pH 3.0 and 30°C
Leucoagaricus meleagris
57.5
-
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
62.1
-
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
70.8
-
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
802
-
ferrocenium ion
native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
812
-
ferrocenium ion
recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.29
-
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
0.32
-
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
20.9
-
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
22.9
-
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
25.5
-
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
Leucoagaricus meleagris
32.5
-
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
44.2
-
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
46.2
-
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
54.4
-
1,4-benzoquinone
recombinant enzyme, at pH 4.0 and 30°C
Leucoagaricus meleagris
54.8
-
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
57.5
-
1,4-benzoquinone
native enzyme, at pH 3.0 and 30°C
Leucoagaricus meleagris
57.5
-
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
62.1
-
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
70.8
-
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
802
-
ferrocenium ion
native enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
812
-
ferrocenium ion
recombinant enzyme, at pH 8.5 and 30°C
Leucoagaricus meleagris
Other publictions for EC 1.1.99.29
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)
739926
Graf
Characterization of three pyra ...
Leucoagaricus meleagris
Appl. Microbiol. Biotechnol.
101
2879-2891
2017
-
-
1
-
-
-
-
36
-
-
1
-
-
8
-
1
1
-
-
-
-
-
36
1
2
-
1
36
1
-
-
1
-
-
-
-
-
3
3
-
-
-
-
-
-
37
-
-
3
-
-
-
3
3
-
-
-
-
36
3
3
-
3
36
3
-
-
-
-
-
-
-
36
36
740401
Gonaus
Analysis of Agaricus meleagris ...
Leucoagaricus meleagris
Enzyme Microb. Technol.
99
57-66
2017
-
-
1
-
6
-
-
40
-
-
1
-
-
2
-
1
1
-
-
-
-
-
4
1
-
-
-
40
-
-
-
1
-
-
-
-
-
1
1
-
6
-
-
-
-
40
-
-
1
-
-
-
1
1
-
-
-
-
4
1
-
-
-
40
-
-
-
-
-
-
-
-
-
-
741362
Gonaus
Transcription analysis of pyra ...
Agaricus bisporus, Agaricus bisporus DSM 3056
Protein Expr. Purif.
119
36-44
2016
-
-
1
-
-
-
-
13
-
-
-
-
-
6
-
-
1
-
-
1
-
1
17
1
1
-
-
13
1
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
13
-
-
-
-
-
-
-
1
-
1
-
1
17
1
1
-
-
13
1
1
1
-
-
-
-
-
13
13
740437
Graf
Reaction of pyranose dehydroge ...
Leucoagaricus meleagris
FEBS J.
282
4218-4241
2015
-
-
1
-
8
-
-
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
8
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741112
Yakovleva
Engineering of pyranose dehydr ...
Leucoagaricus meleagris
Phys. Chem. Chem. Phys.
17
9074-9081
2015
-
-
1
-
-
-
-
-
1
-
-
-
-
3
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739955
Krondorfer
Agaricus meleagris pyranose de ...
Leucoagaricus meleagris
Arch. Biochem. Biophys.
558
111-119
2014
-
-
-
-
1
-
-
-
-
-
1
-
-
3
-
1
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
740391
Cruys-Bagger
A pyranose dehydrogenase-based ...
Leucoagaricus meleagris
Enzyme Microb. Technol.
58-59
68-74
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741223
Graf
Pyranose dehydrogenase ligand ...
Leucoagaricus meleagris
PLoS Comput. Biol.
10
e1003995
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741303
Krondorfer
Engineering of pyranose dehydr ...
Leucoagaricus meleagris
PLoS ONE
9
e91145
2014
-
-
1
-
1
-
-
14
-
-
1
-
-
5
-
1
1
-
-
-
-
-
6
1
-
-
-
12
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
14
-
-
1
-
-
-
1
1
-
-
-
-
6
1
-
-
-
12
-
-
-
-
-
-
-
-
12
12
725611
Graf
Molecular dynamics simulations ...
Leucoagaricus meleagris
J. Comput. Aided Mol. Des.
27
295-304
2013
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726317
Tan
The 1.6 A crystal structure of ...
Leucoagaricus meleagris
PLoS ONE
8
e53567
2013
-
-
1
1
-
-
-
-
-
-
-
4
-
5
-
-
1
-
-
-
-
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
4
-
-
-
1
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739847
Yakovleva
Further insights into the cata ...
Leucoagaricus meleagris
Anal. Chem.
85
9852-9858
2013
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740138
Staudigl
Pyranose dehydrogenase from Ag ...
Agaricus campestris, Agaricus xanthodermus
Biomolecules
3
535-552
2013
-
-
2
-
-
-
-
16
-
-
4
-
-
7
-
2
2
-
-
-
-
-
14
2
-
-
-
16
4
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
16
-
-
4
-
-
-
2
2
-
-
-
-
14
2
-
-
-
16
4
-
-
-
-
-
-
-
16
16
724070
Sygmund
Simple and efficient expressio ...
Leucoagaricus meleagris
Appl. Microbiol. Biotechnol.
94
695-704
2012
-
-
1
-
-
-
-
16
-
-
3
7
-
6
-
1
1
-
-
-
2
-
7
1
-
-
-
16
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
16
-
-
3
7
-
-
1
1
-
-
2
-
7
1
-
-
-
16
-
-
-
-
-
-
-
-
16
16
724834
Yakovleva
-
Recombinant pyranose dehydroge ...
Leucoagaricus meleagris
Electrochem. Commun.
24
120-122
2012
-
-
1
-
-
-
-
-
1
-
-
1
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710969
Pisanelli
Heterologous expression of an ...
Leucoagaricus meleagris, Leucoagaricus meleagris CCBAS 907
Appl. Microbiol. Biotechnol.
86
599-606
2010
-
-
1
-
-
-
-
16
-
-
1
-
-
10
-
1
1
-
-
-
1
-
12
-
-
-
-
16
3
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
16
-
-
1
-
-
-
1
1
-
-
1
-
12
-
-
-
-
16
3
-
-
1
-
-
-
-
16
16
711340
Zafar
Wiring of pyranose dehydrogena ...
Leucoagaricus meleagris
Bioelectrochemistry
80
38-42
2010
-
1
-
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724043
Peterbauer
Pyranose dehydrogenases: Bioch ...
Agaricus xanthodermus, Chlorophyllum rhacodes, Leucoagaricus meleagris
Appl. Microbiol. Biotechnol.
85
837-848
2010
-
-
-
-
-
-
-
14
3
-
3
44
-
5
-
3
-
-
-
-
-
-
44
3
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
14
3
-
3
44
-
-
3
-
-
-
-
-
44
3
-
-
-
14
-
-
-
-
-
-
-
-
14
14
695788
Peterbauer
-
Pyranose dehydrogenases: bioch ...
Agaricus bisporus, Agaricus campestris, Agaricus xanthodermus, Chlorophyllum rhacodes, Leucoagaricus meleagris
Appl. Microbiol. Biotechnol.
146
491-499
2009
-
-
-
-
-
-
-
14
-
-
-
-
-
7
-
5
-
-
-
-
14
-
155
5
-
-
-
14
-
-
-
5
-
-
-
-
-
-
7
-
-
-
-
-
-
42
-
-
-
-
-
-
7
-
-
-
42
-
155
7
-
-
-
42
-
-
-
-
-
-
-
-
-
-
686261
Kittl
Molecular cloning of three pyr ...
Leucoagaricus meleagris
Curr. Genet.
53
117-127
2008
-
1
1
-
-
-
-
-
1
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687883
Sygmund
Characterization of pyranose d ...
Leucoagaricus meleagris
J. Biotechnol.
133
334-342
2008
1
1
-
-
-
-
9
20
1
11
2
-
-
3
-
1
1
-
-
2
-
1
21
1
1
-
1
-
2
1
1
1
-
4
-
1
1
-
1
-
-
-
-
9
-
20
1
11
2
-
-
-
1
1
-
2
-
1
21
1
1
-
1
-
2
1
1
4
-
-
-
-
-
-
686372
Tasca
-
Amperometric biosensors for de ...
Agaricus xanthodermus, Leucoagaricus meleagris
Electroanalysis
19
294-302
2007
-
2
-
-
-
-
-
18
2
-
-
-
-
2
-
-
2
-
-
-
-
-
18
-
-
-
-
-
2
4
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
18
2
-
-
-
-
-
-
2
-
-
-
-
18
-
-
-
-
-
2
4
-
-
-
-
-
-
-
-
686685
Kujawa
Properties of pyranose dehydro ...
Agaricus xanthodermus
FEBS J.
274
879-894
2007
-
1
-
-
-
-
-
21
1
-
1
-
-
4
-
1
1
-
-
-
-
1
22
1
1
-
-
-
3
1
1
1
-
1
-
-
1
-
1
-
-
-
-
-
-
21
1
-
1
-
-
-
1
1
-
-
-
1
22
1
1
-
-
-
3
1
1
1
-
-
-
-
-
-
675469
Sedmera
-
New biotransformations of some ...
Leucoagaricus meleagris
J. Mol. Catal. B
41
32-42
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
644548
Volc
-
C-3 oxidation of non-reducing ...
Leucoagaricus meleagris, Leucoagaricus meleagris CCBAS 907
J. Mol. Catal. B
17
91-100
2002
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
1
1
1
14
-
1
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
1
14
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
644547
Volc
Screening of basidiomycete fun ...
Chlorophyllum rhacodes
Arch. Microbiol.
176
178-186
2001
-
-
-
-
-
1
-
4
1
-
2
-
-
7
-
1
1
-
-
3
1
1
37
1
2
-
-
-
2
-
-
2
-
1
-
-
-
-
2
-
-
1
-
-
-
4
1
-
2
-
-
-
1
1
-
3
1
1
37
1
2
-
-
-
2
-
-
1
-
-
-
-
-
-
644546
Volc
Double oxidation of D-xylose t ...
Agaricus bisporus, Agaricus bisporus 306
Carbohydr. Res.
329
219-225
2000
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
-
1
-
-
3
-
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
3
-
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
644545
Volc
-
C-2 and C-3 oxidation of D-Glc ...
Agaricus bisporus, Agaricus bisporus U3
Carbohydr. Res.
310
151-156
1998
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
-
-
10
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
644544
Volc
Pyranose 2-dehydrogenase, a no ...
Agaricus bisporus
Arch. Microbiol.
167
119-125
1997
1
-
-
-
-
1
5
-
1
-
2
1
-
3
-
1
1
1
-
2
1
1
30
1
1
-
-
-
2
1
-
1
-
1
-
1
-
-
1
-
-
1
-
5
-
-
1
-
2
1
-
-
1
1
-
2
1
1
30
1
1
-
-
-
2
1
-
1
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