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Information on EC 1.1.99.29 - pyranose dehydrogenase (acceptor) and Organism(s) Leucoagaricus meleagris and UniProt Accession Q3L245
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1.1.99.29 pyranose dehydrogenase (acceptor)IUBMB Comments
Requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor. 1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor. Unlike EC 1.1.3.10, pyranose oxidase, this fungal enzyme does not interact with O2 and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars. D-Glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3. The enzyme also acts on 1->4-alpha- and 1->4-beta-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their furanose form.
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Word Map
- 1.1.99.29
- agaricus
- meleagris
-
basidiomycete
- cellobiose
-
flavin-dependent
- synthesis
- bisporus
- biofuel production
- lignocellulose
- analysis
-
pqq-dependent
- benzoquinone
-
coprinopsis
-
glucose-methanol-choline
-
2-oxidase
-
osmium
- pqq
-
litter-decomposing
-
quinohemoprotein
- ferricenium
-
bioanode
-
1.1.3.10
- biotechnology
-
carbohydrate-active
- corynascus
-
bioelectrochemical
- 1,4-benzoquinone
- molecular biology
-
wood-rotting
-
bioelectrocatalysis
- degradation
The taxonomic range for the selected organisms is: Leucoagaricus meleagris
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
=
+
+
=
+
Synonyms
pyranose dehydrogenase, pyranose 2-dehydrogenase, abpdh1, pyranose dehydrogenase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PDH
PDH1
PDH
pyranose dehydrogenase
pyranose-quinone oxidoreductase
-
-
-
-
pyranose:acceptor oxidoreductase
quinone-dependent pyranose dehydrogenase
-
-
-
-
PDH
-
-
-
-
pyranose dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pyranose:acceptor oxidoreductase
Requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor. 1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor. Unlike EC 1.1.3.10, pyranose oxidase, this fungal enzyme does not interact with O2 and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars. D-Glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3. The enzyme also acts on 1->4-alpha- and 1->4-beta-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their furanose form.
CAS REGISTRY NUMBER
COMMENTARY
190606-21-4
-
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
2,3-didehydro-D-glucose + 1,4-benzoquinone
3-dehydro-D-glucose + hydroquinone
-
-
-
?
2-dehydro-D-xylose + 1,4-benzoquinone
2,3-didehydro-D-xylose + hydroquinone
-
-
-
?
2-deoxy-D-galactose + acceptor
?
relative activity towards D-glucose (100%): 31%
-
-
?
2-deoxy-D-glucose + acceptor
?
relative activity towards D-glucose (100%): 27%
-
-
?
2-hydroxymethylphenyl-beta-D-glucopyranoside + acceptor
?
salicin, relative activity towards D-glucose (100%): 78%
-
-
?
3-fluoro-3-deoxy-D-glucose + acceptor
? + reduced acceptor
-
-
-
?
4-hydroxyphenyl-beta-D-glucopyranoside + acceptor
?
arbutin
-
-
?
6-deoxy-D-glucose + acceptor
?
relative activity towards D-glucose (100%): 105%
-
-
?
a pyranoside + acceptor
a 3,4-didehydropyranoside + reduced acceptor
-
-
-
?
alpha,alpha-trehalose + acceptor
3,3'-didehydro-alpha,alpha-trehalose + reduced acceptor
relative activity towards D-glucose (100%): 27%
-
-
?
cellobiitol + acceptor
?
relative activity towards D-glucose (100%): 77%
-
-
?
cellobiose + acceptor
?
relative activity towards D-glucose (100%): 70%
-
-
?
cellobiose + ferrocenium ion
2-dehydro-cellobiose + ferrocene
-
-
-
?
cellotetraose + acceptor
?
relative activity towards D-glucose (100%): 14%
-
-
?
D-allose + acceptor
?
relative activity towards D-glucose (100%): 15%
-
-
?
D-allose + ferricenium ion
? + ferrocene
-
-
-
?
D-galactose + acceptor
2-dehydro-D-galactose + reduced acceptor
relative activity towards D-glucase (100%): 99%
-
-
?
D-glucono-1,5-lactone + acceptor
?
relative activity towards D-glucose (100%): 42%
-
-
?
D-glucose + 1,4-benzoquinone
2,3-didehydro-D-glucose + hydroquinone
-
-
-
?
D-glucose + 2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
3-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
2-dehydro-D-glucose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + acceptor
?
relative activity towards D-glucose (100%): 100%
-
-
?
D-glucose + ferricenium ion
3-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferrocenium ion
3-dehydro-D-glucose + ferrocene
-
-
-
?
D-gulose + acceptor
?
relative activity towards D-glucose (100%): 7%
-
-
?
D-maltose + acceptor
?
relative activity towards D-glucose (100%): 61%
-
-
?
D-mannose + acceptor
2-dehydro-D-mannose + reduced acceptor
-
-
-
?
D-mannose + acceptor
?
relative activity towards D-glucose (100%): 24%
-
-
?
D-mannose + ferrocenium ion
2-dehydro-D-mannose + ferrocene
-
-
-
?
D-ribose + acceptor
?
relative activity towards D-glucose (100%): 19%
-
-
?
D-ribulose + acceptor
?
relative activity towards D-glucose (100%): 17%
-
-
?
D-tagatose + acceptor
?
relative activity towards D-glucoase (100%): 67%
-
-
?
D-talose + acceptor
?
relative activity towards D-glucose (100%): 10%
-
-
?
D-xylose + 1,4-benzoquinone
2-dehydro-D-xylose + hydroquinone
-
-
-
?
D-xylose + acceptor
?
relative activity towards D-glucose (100%): 113%
-
-
?
L-arabinose + acceptor
?
relative activity towards D-glucose (100%): 100%
-
-
?
L-fucose + acceptor
?
relative activity towards D-glucose (100%): 7%
-
-
?
L-glucose + acceptor
?
relative activity towards D-glucose (100%): 42%
-
-
?
L-sorbose + acceptor
?
relative activity towards D-glucose (100%): 5%
-
-
?
lactose + acceptor
?
relative activity towards D-glucose (100%): 15%
-
-
?
lactose + acceptor
lactobiono-1,5-lactone + 2-dehydrolactose + 2,3-didehydrolactose + reduced acceptor
-
-
-
?
maltose + ferricenium ion
? + ferrocene
-
-
-
?
maltotetraose + acceptor
?
relative activity towards D-glucose (100%): 9%
-
-
?
maltotriose + acceptor
?
relative activity towards D-glucose (100%): 12%
-
-
?
melezitose + acceptor
?
relative activity towards D-glucose (100%): 13%
-
-
?
melibiose + acceptor
?
relative activity towards D-glucose (100%): 48%
-
-
?
methyl alpha-D-glucopyranoside + acceptor
?
relative activity towards D-glucose (100%): 107%
-
-
?
methyl alpha-D-mannopyranoside + acceptor
?
relative activity towards D-glucose (100%): 5%
-
-
?
methyl beta-D-glucopyranoside + acceptor
?
relative activity towards D-glucose (100%): 58%
-
-
?
methyl-alpha-D-galactopyranose + acceptor
?
relative activity towards D-glucose (100%): 17%
-
-
?
methyl-alpha-D-glucopyranoside + ferricenium ion
? + ferrocene
-
-
-
?
palatinose + acceptor
?
relative activity towards D-glucose (100%): 89%
-
-
?
pyranoside + acceptor
3,4-didehydropyranoside + reduced acceptor
-
-
-
?
sucrose + acceptor
3'-dehydrosucrose + reduced acceptor
relative activity towards D-glucose (100%): 46%
-
-
?
2-hydroxymethylphenyl-beta-D-glucopyranoside + acceptor
?
salicin, relative activity towards D-glucose (100%): 78%
-
-
?
4-hydroxyphenyl-beta-D-glucopyranoside + acceptor
?
arbutin
-
-
?
6-deoxy-D-glucose + acceptor
?
relative activity towards D-glucose (100%): 105%
-
-
?
a pyranoside + acceptor
a 3,4-didehydropyranoside + reduced acceptor
-
-
-
?
a pyranoside + acceptor
a 3-dehydropyranoside + reduced acceptor
-
-
-
?
alpha,alpha-trehalose + 1,4-benzoquinone
3,3'-didehydro-alpha,alpha-trehalose + hydroquinone
-
quinone-dependent PDH oxidizes alpha,alpha-trehalose at C-3 and C-3, 5% of the activity with D-glucose
with 3-dehydro-alpha,alpha-trehalose as reaction intermediate
-
?
alpha,alpha-trehalose + acceptor
3,3'-didehydro-alpha,alpha-trehalose + reduced acceptor
relative activity towards D-glucose (100%): 27%
-
-
?
cellobiitol + acceptor
?
relative activity towards D-glucose (100%): 77%
-
-
?
cellobiose + 2,6-dichlorophenolindophenol
2-dehydro-cellobiose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
cellobiose + acceptor
?
relative activity towards D-glucose (100%): 70%
-
-
?
cellotetraose + acceptor
?
relative activity towards D-glucose (100%): 14%
-
-
?
D-allose + acceptor
?
relative activity towards D-glucose (100%): 15%
-
-
?
D-allose + ferricenium ion
? + ferrocene
-
-
-
?
D-galactose + acceptor
2-dehydro-D-galactose + reduced acceptor
relative activity towards D-glucase (100%): 99%
-
-
?
D-galactose + benzoquinone
2-dehydro-D-galactose + hydroquinone
-
-
no 2,3-didehydro-d-galactose is detectable
-
?
D-galactose + ferricenium ion
? + ferrocene
-
-
-
?
D-glucono-1,5-lactone + acceptor
?
relative activity towards D-glucose (100%): 42%
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 1,4-benzoquinone
3-dehydro-D-glucose + hydroquinone
-
simultaneous C-2 and C-3 oxidation of free D-glucose
or 2-dehydro-D-glucose
-
?
D-glucose + 2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
3-dehydro-D-glucose + ?
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
2-dehydro-D-glucose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + acceptor
2,3-didehydro-D-glucose + reduced acceptor
-
dioxidation at C2 and C3
-
-
?
D-glucose + acceptor
3-dehydro-D-glucose + reduced acceptor
-
-
-
-
?
D-glucose + acceptor
?
relative activity towards D-glucose (100%): 100%
-
-
?
D-glucose + benzoquinone
2,3-didehydro-D-glucose + hydroquinone
-
pH 3
-
-
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferrocenium ion
2-dehydro-D-glucose + ferrocene
-
-
-
-
?
D-glucose + ferrocenium ion
3-dehydro-D-glucose + ferrocene
-
-
-
-
?
D-gulose + acceptor
?
relative activity towards D-glucose (100%): 7%
-
-
?
D-mannose + ferricenium ion
? + ferrocene
-
-
-
?
D-ribose + acceptor
?
relative activity towards D-glucose (100%): 19%
-
-
?
D-ribulose + acceptor
?
relative activity towards D-glucose (100%): 17%
-
-
?
D-tagatose + acceptor
?
relative activity towards D-glucoase (100%): 67%
-
-
?
D-talose + acceptor
?
relative activity towards D-glucose (100%): 10%
-
-
?
D-xylose + ferricenium ion
? + ferrocene
-
-
-
?
erlose + 1,4-benzoquinone
3-dehydroerlose + hydroquinone
-
quinone-dependent PDH oxidizes erlose at exclusively C-3 of its terminal glucopyranosyl moiety, 9% of the activity with D-glucose
-
-
?
L-glucose + acceptor
?
relative activity towards D-glucose (100%): 42%
-
-
?
L-sorbose + acceptor
?
relative activity towards D-glucose (100%): 5%
-
-
?
lactose + acceptor
?
relative activity towards D-glucose (100%): 15%
-
-
?
lactose + ferricenium ion
? + ferrocene
-
-
-
?
maltose + ferricenium ion
? + ferrocene
-
-
-
?
maltotetraose + acceptor
?
relative activity towards D-glucose (100%): 9%
-
-
?
maltotriose + acceptor
?
relative activity towards D-glucose (100%): 12%
-
-
?
maltotriose + ferricenium ion
? + ferrocene
-
-
-
?
melezitose + acceptor
?
relative activity towards D-glucose (100%): 13%
-
-
?
melibiose + acceptor
?
relative activity towards D-glucose (100%): 48%
-
-
?
melizitose + 1,4-benzoquinone
3-dehydromelizitose + hydroquinone
-
quinone-dependent PDH oxidizes melezitose exclusively at C-3 of its terminal glucopyranosyl moiety, 7% of the activity with D-glucose
-
-
?
methyl alpha-D-glucopyranoside + acceptor
?
relative activity towards D-glucose (100%): 107%
-
-
?
methyl alpha-D-mannopyranoside + acceptor
?
relative activity towards D-glucose (100%): 5%
-
-
?
methyl beta-D-glucopyranoside + acceptor
?
relative activity towards D-glucose (100%): 58%
-
-
?
methyl-alpha-D-galactopyranose + acceptor
?
relative activity towards D-glucose (100%): 17%
-
-
?
methyl-alpha-D-galactopyranoside + 1,4-benzoquinone
methyl-alpha-3-dehydro-D-galactopyranoside + hydroquinone
-
formation of the C-3 carbonyl derivative, 7% of the activity with D-glucose
-
-
?
methyl-alpha-D-glucopyranoside + 1,4-benzoquinone
methyl-alpha-3-dehydro-D-glucopyranoside + hydroquinone
-
formation of the C-3 carbonyl derivative, 126% of the activity with D-glucose
-
-
?
methyl-alpha-D-glucopyranoside + ferricenium ion
? + ferrocene
-
-
-
?
methyl-beta-D-glucopyranoside + 1,4-benzoquinone
methyl-beta-3-dehydro-D-glucopyranoside + hydroquinone
-
formation of the C-3 carbonyl derivative, 20% of the activity with D-glucose
-
-
?
palatinose + acceptor
?
relative activity towards D-glucose (100%): 89%
-
-
?
pyranose + acceptor
2,3-didehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
2-dehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
3-dehydropyranose + reduced acceptor
-
-
-
?
sucrose + 1,4-benzoquinone
3'-dehydrosucrose + hydroquinone
-
quinone-dependent PDH oxidizes sucrose exclusively at C-3 of its terminal glucopyranosyl moiety, 11% of the activity with D-glucose
oxidation of sucrose at C-3 of its terminal glucopyranosyl moiety
-
?
sucrose + acceptor
3'-dehydrosucrose + reduced acceptor
relative activity towards D-glucose (100%): 46%
-
-
?
a pyranoside + acceptor
a 3-dehydropyranoside + reduced acceptor
-
-
-
?
a pyranoside + acceptor
a 3-dehydropyranoside + reduced acceptor
-
-
-
?
a pyranoside + acceptor
a 3-dehydropyranoside + reduced acceptor
-
3-dehydropyranoside or 3,4-didehydropyranoside
-
?
D-galactose + ferricenium ion
? + ferrocene
-
-
-
?
D-galactose + ferrocenium ion
2-dehydro-D-galactose + ferrocene
-
-
-
?
D-galactose + ferrocenium ion
2-dehydro-D-galactose + ferrocene
-
-
-
-
?
D-galactose + ferrocenium ion
2-dehydro-D-galactose + ferrocene
-
-
-
?
D-glucose + 1,4-benzoquinone
2-dehydro-D-glucose + ?
-
-
-
?
D-glucose + acceptor
2-dehydro-D-glucose + reduced acceptor
-
-
-
?
D-glucose + acceptor
2-dehydro-D-glucose + reduced acceptor
the enzyme oxidizes D-glucose at both the C2 and C3 position but the C2 position is the primary site of attack
-
-
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferricenium ion
2-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferrocenium ion
2-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferrocenium ion
2-dehydro-D-glucose + ferrocene
-
-
-
-
?
D-mannose + ferricenium ion
? + ferrocene
-
-
-
?
D-xylose + ferricenium ion
? + ferrocene
-
-
-
?
lactose + ferricenium ion
? + ferrocene
-
-
-
?
maltotriose + ferricenium ion
? + ferrocene
-
-
-
?
pyranose + acceptor
2,3-didehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
2,3-didehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
2-dehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
2-dehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
2-dehydropyranose + reduced acceptor
-
2-dehydropyranose or 1-dehydropyranose or 3-dehydropyranose or 2,3-didehydropyranose
-
?
pyranose + acceptor
3-dehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
3-dehydropyranose + reduced acceptor
-
-
-
?
2-deoxy-D-galactose + acceptor
?
relative activity towards D-glucose (100%): 31%
-
-
?
2-deoxy-D-glucose + acceptor
?
relative activity towards D-glucose (100%): 27%
-
-
?
D-maltose + acceptor
?
relative activity towards D-glucose (100%): 61%
-
-
?
D-mannose + acceptor
?
relative activity towards D-glucose (100%): 24%
-
-
?
D-xylose + acceptor
?
relative activity towards D-glucose (100%): 113%
-
-
?
L-arabinose + acceptor
?
relative activity towards D-glucose (100%): 100%
-
-
?
L-fucose + acceptor
?
relative activity towards D-glucose (100%): 7%
-
-
?
additional information
?
-
O2 is a poor electron acceptor
-
-
?
additional information
?
-
-
extremely broad substrate tolerance
-
-
?
additional information
?
-
-
PDH can oxidise its substrate at the C-1, C-2 or C-3 as well as perform double oxidation at C-1,2, C-2,3 and it has no anomeric specificity. PDH does not show any detectable activity with oxygen
-
-
?
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
2,3-didehydro-D-glucose + 1,4-benzoquinone
3-dehydro-D-glucose + hydroquinone
-
-
-
?
2-dehydro-D-xylose + 1,4-benzoquinone
2,3-didehydro-D-xylose + hydroquinone
-
-
-
?
D-galactose + ferrocenium ion
2-dehydro-D-galactose + ferrocene
-
-
-
?
D-glucose + 1,4-benzoquinone
2,3-didehydro-D-glucose + hydroquinone
-
-
-
?
D-glucose + acceptor
2-dehydro-D-glucose + reduced acceptor
the enzyme oxidizes D-glucose at both the C2 and C3 position but the C2 position is the primary site of attack
-
-
?
D-glucose + ferricenium ion
3-dehydro-D-glucose + ferrocene
-
-
-
?
D-glucose + ferrocenium ion
3-dehydro-D-glucose + ferrocene
-
-
-
?
D-xylose + 1,4-benzoquinone
2-dehydro-D-xylose + hydroquinone
-
-
-
?
lactose + acceptor
lactobiono-1,5-lactone + 2-dehydrolactose + 2,3-didehydrolactose + reduced acceptor
-
-
-
?
pyranose + acceptor
2,3-didehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
3-dehydropyranose + reduced acceptor
-
-
-
?
pyranoside + acceptor
3,4-didehydropyranoside + reduced acceptor
-
-
-
?
D-glucose + acceptor
2,3-didehydro-D-glucose + reduced acceptor
-
dioxidation at C2 and C3
-
-
?
D-glucose + ferrocenium ion
3-dehydro-D-glucose + ferrocene
-
-
-
-
?
a pyranoside + acceptor
a 3-dehydropyranoside + reduced acceptor
-
-
-
?
a pyranoside + acceptor
a 3-dehydropyranoside + reduced acceptor
-
3-dehydropyranoside or 3,4-didehydropyranoside
-
?
pyranose + acceptor
2-dehydropyranose + reduced acceptor
-
-
-
?
pyranose + acceptor
2-dehydropyranose + reduced acceptor
-
2-dehydropyranose or 1-dehydropyranose or 3-dehydropyranose or 2,3-didehydropyranose
-
?
additional information
?
-
O2 is a poor electron acceptor
-
-
?
additional information
?
-
-
PDH can oxidise its substrate at the C-1, C-2 or C-3 as well as perform double oxidation at C-1,2, C-2,3 and it has no anomeric specificity. PDH does not show any detectable activity with oxygen
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4+
-
at 0.1-1 M in 20 mM sodium phosphate buffer pH 7.0, not due to increased ionic strenth
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0791
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
18.3
D-allose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
137
D-sorbose
ferricenium ion as electron acceptor
137
L-sorbose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
10.3
maltose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.66
methyl-alpha-D-glucopyranoside
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.92
2,5-chloro-1,4-benzoquinone
-
at 30°C with 50 mM glucose as susbtrate
0.55
2-chloro-1,4-benzoquinone
-
at 30°C with 50 mM glucose as susbtrate
0.22
3,5-di-tert-butyl-1,4-benzoquinone
-
at 30°C with 50 mM glucose as susbtrate
137
D-sorbose
ferricenium ion as electron acceptor
0.18
methyl-1,4-benzoquinone
-
at 30°C with 50 mM glucose as susbtrate
10.8
xylobiose
ferricenium ion as electron acceptor
1.03
1,4-benzoquinone
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0
1.38
1,4-benzoquinone
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
1.38
1,4-benzoquinone
wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C
1.82
1,4-benzoquinone
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0
3.64
1,4-benzoquinone
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.02
2,6-dichlorophenolindophenol
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.14
2,6-dichlorophenolindophenol
wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.55
2-chloro-1,4-benzoquinone
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0
0.55
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
0.61
2-chloro-1,4-benzoquinone
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0
0.62
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
5.72
cellobiose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
6.82
cellobiose
ferricenium ion as electron acceptor
6.82
cellobiose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
153
D-fructose
ferricenium ion as electron acceptor
153
D-fructose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.64
D-galactose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.86
D-galactose
mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C
1.02
D-galactose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
1.05
D-galactose
ferricenium ion as electron acceptor
1.05
D-galactose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
1.05
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
1.05
D-galactose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
1.07
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
1.07
D-galactose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
3.55
D-galactose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
5.29
D-galactose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
0.69
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
0.69
D-glucose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
0.82
D-glucose
ferricenium ion as electron acceptor
0.82
D-glucose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
0.82
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
0.82
D-glucose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.82
D-glucose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.86
D-glucose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
1.94
D-glucose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
3.85
D-glucose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
8.61
D-maltose
ferricenium ion as electron acceptor
8.61
D-maltose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
94
D-mannose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
108
D-mannose
ferricenium ion as electron acceptor
108
D-mannose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
380
D-mannose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
59.7
D-ribose
ferricenium ion as electron acceptor
59.7
D-ribose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
79.1
D-talose
ferricenium ion as electron acceptor
79.1
D-talose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
1.03
D-xylose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
1.92
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
1.93
D-xylose
ferricenium ion as electron acceptor
1.93
D-xylose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
1.93
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
1.93
D-xylose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
2.39
D-xylose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.13
ferricenium ion
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5
0.161
ferricenium ion
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.22
ferricenium ion
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5
0.1
ferrocenium ion
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 8.5 and 30°C
0.1
ferrocenium ion
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
0.11
ferrocenium ion
mutant enzyme N75G/N175Q, at pH 7.5 and 30°C
0.16
ferrocenium ion
wild type enzyme, with D-glucose as cosubstrate, at pH 8.5 and 30°C
0.29
ferrocenium ion
mutant enzyme N75G/N252Q, at pH 7.5 and 30°C
0.37
ferrocenium ion
mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C
0.44
L-arabinose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
0.49
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
0.54
L-arabinose
ferricenium ion as electron acceptor
0.54
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
0.54
L-arabinose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.74
L-arabinose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
76.7
lactose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
113.9
lactose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
128
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
128
lactose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
134
lactose
ferricenium ion as electron acceptor
134
lactose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
134
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
134
lactose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
395.9
lactose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
62.5
maltotriose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
156
maltotriose
ferricenium ion as electron acceptor
156
maltotriose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.095
O2
wild type enzyme, with D-glucose as cosubstrate, at pH 7.4 and 30°C
0.5
O2
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 7.4 and 30°C
10.8
xylobiose
ferricenium ion as electron acceptor
10.8
xylobiose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.0325
1,4-benzoquinone
isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C
1.88
1,4-benzoquinone
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.0132
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.109
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C
6.82
cellobiose
ferricenium ion as electron acceptor
113
D-allose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
181
D-allose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
153
D-fructose
ferricenium ion as electron acceptor
1.05
D-galactose
ferricenium ion as electron acceptor
29.7
D-galactose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
40.1
D-galactose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.53
D-glucose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.82
D-glucose
ferricenium ion as electron acceptor
3.28
D-glucose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
8.61
D-maltose
ferricenium ion as electron acceptor
34.9
D-mannose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
108
D-mannose
ferricenium ion as electron acceptor
185
D-mannose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
59.7
D-ribose
ferricenium ion as electron acceptor
79.1
D-talose
ferricenium ion as electron acceptor
1.93
D-xylose
ferricenium ion as electron acceptor
9.34
D-xylose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
17
D-xylose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.0103
ferricenium ion
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.0201
ferricenium ion
isoform PDH2, at pH 8.5 and 30°C
0.54
L-arabinose
ferricenium ion as electron acceptor
134
lactose
ferricenium ion as electron acceptor
235
lactose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
2288
lactose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
2.22
maltose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
11.6
maltose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
54.6
maltotriose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
154
maltotriose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
156
maltotriose
ferricenium ion as electron acceptor
0.95
methyl-alpha-D-glucopyranoside
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
2
methyl-alpha-D-glucopyranoside
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.57
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
18.4
D-allose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
15.7
D-sorbose
ferricenium ion as electron acceptor
15.7
L-sorbose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
44.7
maltose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
41.5
methyl-alpha-D-glucopyranoside
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
38.4
cellobiose
ferricenium ion as electron acceptor
16.5
D-fructose
ferricenium ion as electron acceptor
43.2
D-maltose
ferricenium ion as electron acceptor
31.4
D-ribose
ferricenium ion as electron acceptor
15.7
D-sorbose
ferricenium ion as electron acceptor
21.3
D-talose
ferricenium ion as electron acceptor
37.2
L-arabinose
ferricenium ion as electron acceptor
50.4
xylobiose
ferricenium ion as electron acceptor
13.6
1,4-benzoquinone
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C
59
1,4-benzoquinone
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0
65.4
1,4-benzoquinone
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
65.4
1,4-benzoquinone
wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C
76
1,4-benzoquinone
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0
2.8
2,6-dichlorophenolindophenol
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C
40.7
2,6-dichlorophenolindophenol
wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C
12.9
2-chloro-1,4-benzoquinone
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0
12.9
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
15.1
2-chloro-1,4-benzoquinone
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0
15.1
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
34.7
cellobiose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
38.4
cellobiose
ferricenium ion as electron acceptor
38.4
cellobiose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
16.5
D-fructose
ferricenium ion as electron acceptor
16.5
D-fructose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
28.9
D-galactose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
34.3
D-galactose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
38.9
D-galactose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
39.3
D-galactose
mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C
46.6
D-galactose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
47.3
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
47.3
D-galactose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
48.5
D-galactose
ferricenium ion as electron acceptor
48.5
D-galactose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
48.5
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
48.5
D-galactose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
27.4
D-glucose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
37.8
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
37.8
D-glucose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
42.2
D-glucose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
45.9
D-glucose
ferricenium ion as electron acceptor
45.9
D-glucose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
45.9
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
45.9
D-glucose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
48.06
D-glucose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
49.7
D-glucose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
43.2
D-maltose
ferricenium ion as electron acceptor
43.2
D-maltose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
26.5
D-mannose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
27
D-mannose
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
29.3
D-mannose
ferricenium ion as electron acceptor
29.3
D-mannose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
31.4
D-ribose
ferricenium ion as electron acceptor
31.4
D-ribose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
21.3
D-talose
ferricenium ion as electron acceptor
21.3
D-talose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
41.5
D-xylose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
43.4
D-xylose
ferricenium ion as electron acceptor
43.4
D-xylose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
43.4
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
43.4
D-xylose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
51.3
D-xylose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
62.4
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
104
ferricenium ion
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5
130
ferricenium ion
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
203
ferricenium ion
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5
26
ferrocenium ion
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 8.5 and 30°C
44.8
ferrocenium ion
mutant enzyme N75G/N175Q, at pH 7.5 and 30°C
50.7
ferrocenium ion
mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C
54.2
ferrocenium ion
mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C
54.6
ferrocenium ion
mutant enzyme N75G/N252Q, at pH 7.5 and 30°C
130
ferrocenium ion
wild type enzyme, with D-glucose as cosubstrate, at pH 8.5 and 30°C
34.7
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
37.2
L-arabinose
ferricenium ion as electron acceptor
37.2
L-arabinose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
37.2
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
37.2
L-arabinose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
45.7
L-arabinose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
24.7
lactose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
31.9
lactose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
33.7
lactose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
39.6
lactose
ferricenium ion as electron acceptor
39.6
lactose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
39.6
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
39.6
lactose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
41
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
41
lactose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
23.6
maltotriose
ferricenium ion as electron acceptor
23.6
maltotriose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
35.9
maltotriose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
50.4
xylobiose
ferricenium ion as electron acceptor
50.4
xylobiose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
3.57
1,4-benzoquinone
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
23.4
1,4-benzoquinone
isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C
4.28
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C
5.32
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
35.3
D-allose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
40.2
D-allose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
19.3
D-galactose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
48.5
D-galactose
ferricenium ion as electron acceptor
137
D-galactose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
8.16
D-glucose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
35.7
D-glucose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
45.9
D-glucose
ferricenium ion as electron acceptor
29.3
D-mannose
ferricenium ion as electron acceptor
34.7
D-mannose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
109
D-mannose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
29.5
D-xylose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
43.4
D-xylose
ferricenium ion as electron acceptor
146
D-xylose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
9.86
ferricenium ion
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
48.1
ferricenium ion
isoform PDH2, at pH 8.5 and 30°C
39.6
lactose
ferricenium ion as electron acceptor
75.3
lactose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
209
lactose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.48
maltose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
7.63
maltose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
16.3
maltotriose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
21.2
maltotriose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
23.6
maltotriose
ferricenium ion as electron acceptor
1
methyl-alpha-D-glucopyranoside
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
85
methyl-alpha-D-glucopyranoside
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
94.6
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
5.6
cellobiose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
1.01
D-allose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.11
D-fructose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
5
D-maltose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.52
D-ribose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.27
D-talose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.11
L-sorbose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
4.34
maltose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
62.9
methyl-alpha-D-glucopyranoside
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
4.7
xylobiose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
4
1,4-benzoquinone
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C
47.4
1,4-benzoquinone
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
47.4
1,4-benzoquinone
wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C
57.3
1,4-benzoquinone
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0
57.5
1,4-benzoquinone
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0
140
2,6-dichlorophenolindophenol
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C
290.7
2,6-dichlorophenolindophenol
wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C
20.9
2-chloro-1,4-benzoquinone
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0
20.9
2-chloro-1,4-benzoquinone
recombinant enzyme, at pH 5.0 and 30°C
25.5
2-chloro-1,4-benzoquinone
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0
25.5
2-chloro-1,4-benzoquinone
native enzyme, at pH 5.0 and 30°C
5.5
D-galactose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
44.2
D-galactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
44.2
D-galactose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
45.7
D-galactose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
46.2
D-galactose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
46.2
D-galactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
46.2
D-galactose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
53.6
D-galactose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
7.1
D-glucose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
51.5
D-glucose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
54.8
D-glucose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
54.8
D-glucose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
55.9
D-glucose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
57.5
D-glucose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
57.5
D-glucose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
57.5
D-glucose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.27
D-mannose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.282
D-mannose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
21.5
D-xylose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
22.9
D-xylose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
22.9
D-xylose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
22.9
D-xylose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
32.5
D-xylose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
40.3
D-xylose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
802
ferricenium ion
native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5
812
ferricenium ion
isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C
923
ferricenium ion
recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5
260
ferrocenium ion
mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 8.5 and 30°C
812.5
ferrocenium ion
wild type enzyme, with D-glucose as cosubstrate, at pH 8.5 and 30°C
61.8
L-arabinose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
62.1
L-arabinose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
62.1
L-arabinose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
62.1
L-arabinose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
70.8
L-arabinose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
0.1
lactose
mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
0.28
lactose
recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
0.29
lactose
native enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5
0.29
lactose
using ferrocenium ion as cosubstrate, native enzyme, at pH 8.5 and 30°C
0.29
lactose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.32
lactose
using ferrocenium ion as cosubstrate, recombinant enzyme, at pH 8.5 and 30°C
0.32
lactose
wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C
0.439
lactose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.15
maltotriose
with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication
0.574
maltotriose
isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
1.89
1,4-benzoquinone
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
780
1,4-benzoquinone
isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C
38.9
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C
532
2,2'-azino-bis[3-ethylbenzothiazoline]-6-sulfonic acid
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
0.195
D-allose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.356
D-allose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.65
D-galactose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
3.41
D-galactose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
2.48
D-glucose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
67.4
D-glucose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.188
D-mannose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
3.12
D-mannose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
3.16
D-xylose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
8.59
D-xylose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
986
ferricenium ion
isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C
2400
ferricenium ion
isoform PDH2, at pH 8.5 and 30°C
0.0913
lactose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.32
lactose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.216
maltose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.658
maltose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.106
maltotriose
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
0.388
maltotriose
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
1.05
methyl-alpha-D-glucopyranoside
isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
42.5
methyl-alpha-D-glucopyranoside
isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.1
substrate: D-sorbose, ferricenium ion as electron acceptor
14.9
substrate: D-fructose, ferricenium ion as electron acceptor
19.2
substrate: D-talose, ferricenium ion as electron acceptor
21.3
substrate: maltotriose, ferricenium ion as electron acceptor
26.4
substrate: D-mannose, ferricenium ion as electron acceptor
28.2
substrate: D-ribose, ferricenium ion as electron acceptor
33.5
substrate: L-arabinose, ferricenium ion as electron acceptor
34.5
substrate: cellobiose ferricenium ion as electron acceptor
35.6
substrate: lactose, ferricenium ion as electron acceptor
38.9
substrate: D-maltose, ferricenium ion as electron acceptor
39.1
substrate: D-xylose, ferricenium ion as electron acceptor
41.4
substrate: D-glucose, ferricenium ion as electron acceptor
43.7
substrate: D-galactose, ferricenium ion as electron acceptor
45.4
substrate: xylobiose, ferricenium ion as electron acceptor
14.1
substrate: D-sorbose, ferricenium ion as electron acceptor
14.9
substrate: D-fructose, ferricenium ion as electron acceptor
19.2
substrate: D-talose, ferricenium ion as electron acceptor
21.3
substrate: maltotriose, ferricenium ion as electron acceptor
26.4
substrate: D-mannose, ferricenium ion as electron acceptor
28.2
substrate: D-ribose, ferricenium ion as electron acceptor
33.5
substrate: L-arabinose, ferricenium ion as electron acceptor
34.5
substrate: cellobiose ferricenium ion as electron acceptor
35.6
substrate: lactose, ferricenium ion as electron acceptor
38.9
substrate: D-maltose, ferricenium ion as electron acceptor
39.1
substrate: D-xylose, ferricenium ion as electron acceptor
41.4
substrate: D-glucose, ferricenium ion as electron acceptor
43.7
substrate: D-galactose, ferricenium ion as electron acceptor
45.4
substrate: xylobiose, ferricenium ion as electron acceptor
additional information
additional information
the recombinant enzyme from Aspergillus nidulans crude extract shows a specific activity of 13.5 units/mg using D-glucose as substrate, at 30°C in phosphate buffer, pH 7.5. The recombinant 4.1fold purified enzyme from Aspergillus nidulans shows a specific activity of 55.9 units/mg using D-glucose as substrate, at 30°C in phosphate buffer, pH 7.5
additional information
-
the recombinant enzyme from Aspergillus nidulans crude extract shows a specific activity of 13.5 units/mg using D-glucose as substrate, at 30°C in phosphate buffer, pH 7.5. The recombinant 4.1fold purified enzyme from Aspergillus nidulans shows a specific activity of 55.9 units/mg using D-glucose as substrate, at 30°C in phosphate buffer, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
in 0.1 M ethanolamine buffer, applied potential + 300 mV vs. Ag-AgCl, 1 mM D-glucose, flow rate 1.0 mL/min
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 10
-
depending on the electron acceptor and with d-glucose as electron donor, has 2 pH optima for some substrates
7 - 10.5
-
depending on the buffer, highest biosensor response in 0.1 M ethanolamine buffer, applied potential + 300 mV vs. Ag-AgCl, 1 mM glucose, flow rate 1.0 ml/min
7 - 8
-
in PBS, applied potential + 300 mV vs. Ag-AgCl, 1 mM glucose, flow rate 1.0 ml/min
8 - 9
-
in Tris, applied potential + 300 mV vs. Ag-AgCl, 1 mM glucose, flow rate 1.0 ml/min
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
production of PDH is limited to the family of Agaricaceae
evolution
production of PDH is limited to the family of Agaricaceae
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). PDH1_LEUMG
602
0
64684
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycoprotein
the recombinant protein contains approximately 7% N-linked carbohydrate moiety
glycoprotein
the level of glycosylation of recombinant enzyme is approximately 30%
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microseeding, using 50 mM KH2PO4, 5% (v/v) 2-methyl-2,4-pentanediol, and 20% (w/v) polyethylene glycol 8000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H103A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 10 compared to the wild type enzyme
H103Y
the mutant reveals a 5fold increase of the oxygen reactivity compared to the wild type enzyme
H512A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100000 compared to the wild type enzyme
H556A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100 compared to the wild type enzyme
H556N
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 1000 compared to the wild type enzyme
N175Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N175Q/N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N75G
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N75G/N175Q/N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N75G/N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
Q392A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 10 compared to the wild type enzyme
V511F
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100 compared to the wild type enzyme
V511W
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 10 compared to the wild type enzyme
Y510A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100 compared to the wild type enzyme
H103Y
-
the mutant is still able to bind FAD (non-covalently) and perform catalysis but steady-state kinetic parameters for several substrates are negatively affected
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66 - 73
isoform PDH1 shows its highest thermal stability between pH values 5.0 and 6.0, with maximum melting temperature at 73.5°C and pH 5.0
66 - 73
66 - 73
isoform PDH2 shows a significantly reduced thermostability over the whole pH range with a maximum melting temperature of 66.5°C at pH 6.0
66 - 73
isoform PDH3 shows its highest thermal stability between pH values 5.0 and 6.0, with maximum melting temperature at 73°C and pH 6.0
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Superose12 gel filtration
ammonium sulfate precipitation, Ni2+-charged chelating Sepharose column chromatography, and DEAE Sepharose column chromatography
anion exchange column chromatography and Superdex 75 gel filtration
cross-flow filtration, hydrophobic interaction and immobilized metal affinity chromatography
DEAE Sepharose column chromatography and phenyl Sepharose column chromatography
EMD DEAE 650 S column chromatography and Source 15 PHE column chromatography
hydrophobic interaction chromatography and anion exchange chromatography
phenyl Sepharose column chromatography, DEAE Sepharose column chromatography, and gel filtration
using ammonium sulfate fractionation, ion-exchange and hydrophobic interaction chromatography
ammonium sulfate precipitation, Ni2+-charged chelating Sepharose column chromatography, and DEAE Sepharose column chromatography
using ammonium sulfate fractionation, ion-exchange and hydrophobic interaction chromatography
using DEAE-Sephacel anion exchange chromatography and FPLC on phenyl-superose HR 10/10, Mono Q HR 5/5 and superose 12 HR 30/10 chromatography
-
using ammonium sulfate fractionation, ion-exchange and hydrophobic interaction chromatography
using ammonium sulfate fractionation, ion-exchange and hydrophobic interaction chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expressed in Saccharomyces cerevisiae and Pichia pastoris strain X33
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
generally low and probably constitutive transcription level and a moderate increase in transcription rate upon carbon depletion. pdh1 shows a significantly higher transcription rate compared to pdh2 and pdh3, and stress-related induction upon oxygen deprivation
generally low and probably constitutive transcription level and a moderate increase in transcription rate upon carbon depletion. pdh1 shows a significantly higher transcription rate compared to pdh2 and pdh3, and stress-related induction upon oxygen deprivation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars
biofuel production
pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures
molecular biology
gene expression analysis using PCR, pdh1 expression is upregulated upon exhaustion of the carbon source and appears to be additionally regulated under conditions of oxygen limitation, PDH production is highest on cellobiose and very low on fructose
synthesis
pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals
analysis
pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars
biofuel production
pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures
biotechnology
molecular biology
synthesis
biotechnology
-
PDH is an alternative to pyranose oxidase for applications in biotechnology or biofuel cells, electrical wiring of the enzyme bound to graphite rod electrodes is studied
biotechnology
-
PDH can be very efficiently wired with osmium polymers having E°' values close to that of PDH
molecular biology
gene expression analysis using PCR, pdh2 is constitutively expressed, PDH production is highest on cellobiose and very low on fructose
molecular biology
gene expression analysis using PCR, pdh3 is constitutively expressed, PDH production is highest on cellobiose and very low on fructose
synthesis
-
PDH catalysis with 1,4-benzoquinone as an oxidant provides biocatalytic sugar chemistry with a new convenient tool for high yield production of 3-keto-oligosaccharides and 3-keto-glycosides
synthesis
pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Volc, J.; Sedmera, P.; Halada, P.; Daniel, G.; Pikyrlov, V.; Haltrich, D.
C-3 oxidation of non-reducing sugars by a fungal pyranose dehydrogenase: spectral characterization
J. Mol. Catal. B
17
91-100
2002
Leucoagaricus meleagris, Leucoagaricus meleagris CCBAS 907
-
Sedmera, P.; Halada, P.; Kubatova, E.; Haltrich, D.; Prikrylova, V.; Volc, J.
New biotransformations of some reducing sugars to the corresponding (di)dehydro(glycosyl) aldoses or aldonic acids using fungal pyranose dehydrogenase
J. Mol. Catal. B
41
32-42
2006
Leucoagaricus meleagris
-
Kittl, R.; Sygmund, C.; Halada, P.; Volc, J.; Divne, C.; Haltrich, D.; Peterbauer, C.K.
Molecular cloning of three pyranose dehydrogenase-encoding genes from Agaricus meleagris and analysis of their expression by real-time RT-PCR
Curr. Genet.
53
117-127
2008
Leucoagaricus meleagris, Leucoagaricus meleagris (Q3L245)
Tasca, F.; Timur, S.; Ludwig, R.; Haltrich, D.; Volc, J.; Antiochia, R.; Gorton, L.
Amperometric biosensors for detection of sugars based on the electrical wiring of different pyranose oxidases and pyranose dehydrogenases with osmium redox polymer on graphite electrodes
Electroanalysis
19
294-302
2007
Leucoagaricus meleagris, Agaricus xanthodermus (Q3L1D2)
-
Sygmund, C.; Kittl, R.; Volc, J.; Halada, P.; Kubatova, E.; Haltrich, D.; Peterbauer, C.K.
Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose
J. Biotechnol.
133
334-342
2008
Leucoagaricus meleagris
Peterbauer, C.; Volc, J.
Pyranose dehydrogenases: biochemical features and perspectives of technological applications
Appl. Microbiol. Biotechnol.
146
491-499
2009
Agaricus bisporus (Q3L1D1), Agaricus campestris, Agaricus xanthodermus (Q3L1D2), Chlorophyllum rhacodes, Leucoagaricus meleagris (Q0R4L2), Leucoagaricus meleagris (Q3L243), Leucoagaricus meleagris (Q3L245)
-
Pisanelli, I.; Kujawa, M.; Gschnitzer, D.; Spadiut, O.; Seiboth, B.; Peterbauer, C.
Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding gene in Aspergillus spp. and characterization of the recombinant enzyme
Appl. Microbiol. Biotechnol.
86
599-606
2010
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris, Leucoagaricus meleagris CCBAS 907 (Q3L245)
Zafar, M.N.; Tasca, F.; Boland, S.; Kujawa, M.; Patel, I.; Peterbauer, C.K.; Leech, D.; Gorton, L.
Wiring of pyranose dehydrogenase with osmium polymers of different redox potentials
Bioelectrochemistry
80
38-42
2010
Leucoagaricus meleagris
Peterbauer, C.; Volc, J.
Pyranose dehydrogenases: Biochemical features and perspectives of technological applications
Appl. Microbiol. Biotechnol.
85
837-848
2010
Agaricus xanthodermus (Q3L1D2), Chlorophyllum rhacodes, Leucoagaricus meleagris (Q3L245)
Sygmund, C.; Gutmann, A.; Krondorfer, I.; Kujawa, M.; Glieder, A.; Pscheidt, B.; Haltrich, D.; Peterbauer, C.; Kittl, R.
Simple and efficient expression of Agaricus meleagris pyranose dehydrogenase in Pichia pastoris
Appl. Microbiol. Biotechnol.
94
695-704
2012
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Yakovleva, M.; Killyni, A.; Ortiz, R.; Schulz, C.; MacAodha, D.; Conghaile, P.; Leech, D.; Popescu, I.; Gonaus, C.; Peterbauer, C.; Gorton, L.
Recombinant pyranose dehydrogenase - A versatile enzyme possessing both mediated and direct electron transfer
Electrochem. Commun.
24
120-122
2012
Leucoagaricus meleagris
-
Graf, M.; Bren, U.; Haltrich, D.; Oostenbrink, C.
Molecular dynamics simulations give insight into D-glucose dioxidation at C2 and C3 by Agaricus meleagris pyranose dehydrogenase
J. Comput. Aided Mol. Des.
27
295-304
2013
Leucoagaricus meleagris
Tan, T.; Spadiut, O.; Wongnate, T.; Sucharitakul, J.; Krondorfer, I.; Sygmund, C.; Haltrich, D.; Chaiyen, P.; Peterbauer, C.; Divne, C.
The 1.6 A crystal structure of pyranose dehydrogenase from Agaricus meleagris rationalizes substrate specificity and reveals a flavin intermediate
PLoS ONE
8
e53567
2013
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Yakovleva, M.E.; Killyeni, A.; Seubert, O.; O Conghaile, P.; Macaodha, D.; Leech, D.; Gonaus, C.; Popescu, I.C.; Peterbauer, C.K.; Kjellstroem, S.; Gorton, L.
Further insights into the catalytical properties of deglycosylated pyranose dehydrogenase from Agaricus meleagris recombinantly expressed in Pichia pastoris
Anal. Chem.
85
9852-9858
2013
Leucoagaricus meleagris
Graf, M.M.; Weber, S.; Kracher, D.; Kittl, R.; Sygmund, C.; Ludwig, R.; Peterbauer, C.; Haltrich, D.
Characterization of three pyranose dehydrogenase isoforms from the litter-decomposing basidiomycete Leucoagaricus meleagris (syn. Agaricus meleagris)
Appl. Microbiol. Biotechnol.
101
2879-2891
2017
Leucoagaricus meleagris (Q0R4L2), Leucoagaricus meleagris (Q3L243), Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Krondorfer, I.; Brugger, D.; Paukner, R.; Scheiblbrandner, S.; Pirker, K.F.; Hofbauer, S.; Furtmueller, P.G.; Obinger, C.; Haltrich, D.; Peterbauer, C.K.
Agaricus meleagris pyranose dehydrogenase: influence of covalent FAD linkage on catalysis and stability
Arch. Biochem. Biophys.
558
111-119
2014
Leucoagaricus meleagris
Cruys-Bagger, N.; Badino, S.F.; Tokin, R.; Gontsarik, M.; Fathalinejad, S.; Jensen, K.; Toscano, M.D.; Sorensen, T.H.; Borch, K.; Tatsumi, H.; Vaeljamaee, P.; Westh, P.
A pyranose dehydrogenase-based biosensor for kinetic analysis of enzymatic hydrolysis of cellulose by cellulases
Enzyme Microb. Technol.
58-59
68-74
2014
Leucoagaricus meleagris
Gonaus, C.; Maresch, D.; Schropp, K.; O Conghaile, P.; Leech, D.; Gorton, L.; Peterbauer, C.K.
Analysis of Agaricus meleagris pyranose dehydrogenase N-glycosylation sites and performance of partially non-glycosylated enzymes
Enzyme Microb. Technol.
99
57-66
2017
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Graf, M.M.; Sucharitakul, J.; Bren, U.; Chu, D.B.; Koellensperger, G.; Hann, S.; Furtmueller, P.G.; Obinger, C.; Peterbauer, C.K.; Oostenbrink, C.; Chaiyen, P.; Haltrich, D.
Reaction of pyranose dehydrogenase from Agaricus meleagris with its carbohydrate substrates
FEBS J.
282
4218-4241
2015
Leucoagaricus meleagris (Q3L245)
Yakovleva, M.E.; Gonaus, C.; Schropp, K.; OConghaile, P.; Leech, D.; Peterbauer, C.K.; Gorton, L.
Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells
Phys. Chem. Chem. Phys.
17
9074-9081
2015
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Graf, M.M.; Zhixiong, L.; Bren, U.; Haltrich, D.; van Gunsteren, W.F.; Oostenbrink, C.
Pyranose dehydrogenase ligand promiscuity: a generalized approach to simulate monosaccharide solvation, binding, and product formation
PLoS Comput. Biol.
10
e1003995
2014
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Krondorfer, I.; Lipp, K.; Brugger, D.; Staudigl, P.; Sygmund, C.; Haltrich, D.; Peterbauer, C.K.
Engineering of pyranose dehydrogenase for increased oxygen reactivity
PLoS ONE
9
e91145
2014
Leucoagaricus meleagris (Q3L245), Leucoagaricus meleagris
Peterbauer, C.K.
Pyranose dehydrogenases Rare enzymes for electrochemistry and biocatalysis
Bioelectrochemistry
132
107399
2020
Agaricus bisporus (Q3L1D1), Agaricus campestris (V5NDL4), Agaricus xanthodermus (V5NC32), Chlorophyllum rhacodes, Leucoagaricus meleagris (Q0R4L2), Leucoagaricus meleagris (Q3L243), Leucoagaricus meleagris (Q3L245)
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