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Information on EC 1.2.3.15 - (methyl)glyoxal oxidase for references in articles please use BRENDA:EC1.2.3.15
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EC Tree
IUBMB Comments The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis.
The expected taxonomic range for this enzyme is: Phanerochaete chrysosporium
Synonyms
GLOX, GLX, Glx1, GLX2, methylglyoxal oxidase,
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GLOX
-
GLX
-
Glx1
-
-
gene name
-
Glx1
gene name; gene name; gene name
-
GLX2
-
-
gene name
-
methylglyoxal oxidase
-
methylglyoxal oxidase
-
-
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2-oxopropanal + H2O + O2 = pyruvate + H2O2
(2)
-
-
-
glyoxal + H2O + O2 = glyoxylate + H2O2
(1)
-
-
-
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(methyl)glyoxal:oxygen oxidoreductase
The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis.
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2-oxopropanal + H2O + O2
pyruvate + H2O2
acetaldehyde + H2O + O2
?
acetaldehyde + H2O + O2
acetate + H2O2
61% activity compared to methylglyoxal
-
-
?
acetol + H2O + O2
?
4% activity compared to methylglyoxal
-
-
?
dihydroxyacetone + H2O + O2
?
DL-glyceraldehyde + H2O + O2
?
formaldehyde + H2O + O2
?
-
3.6% activity compared to methylglyoxal
-
-
?
formaldehyde + H2O + O2
formate + H2O2
54% activity compared to methylglyoxal
-
-
?
glycolaldehyde + H2O + O2
?
-
8.1% activity compared to methylglyoxal
-
-
?
glycolaldehyde + H2O + O2
hydroxyacetate + H2O2
69% activity compared to methylglyoxal
-
-
?
glyoxal + H2O + O2
glyoxylate + H2O2
glyoxylic acid + H2O + O2
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
additional information
?
-
less than 2% activity with D-cellobiose, D-glucose, D-galactose, D-xylose, glycerol, hydroxypyruvic acid, pyruvic acid, ethylene glycol, oxalic acid, and methanol
-
-
-
2-oxopropanal + H2O + O2
pyruvate + H2O2
-
-
-
-
?
2-oxopropanal + H2O + O2
pyruvate + H2O2
-
-
-
-
?
acetaldehyde + H2O + O2
?
-
5.7% activity compared to methylglyoxal
-
-
?
acetaldehyde + H2O + O2
?
-
5.7% activity compared to methylglyoxal
-
-
?
dihydroxyacetone + H2O + O2
?
-
1.6% activity compared to methylglyoxal
-
-
?
dihydroxyacetone + H2O + O2
?
26% activity compared to methylglyoxal
-
-
?
dihydroxyacetone + H2O + O2
?
-
1.6% activity compared to methylglyoxal
-
-
?
DL-glyceraldehyde + H2O + O2
?
-
1.1% activity compared to methylglyoxal
-
-
?
DL-glyceraldehyde + H2O + O2
?
25% activity compared to methylglyoxal
-
-
?
glyoxal + H2O + O2
?
-
3.3% activity compared to methylglyoxal
-
-
?
glyoxal + H2O + O2
?
45% activity compared to methylglyoxal
-
-
?
glyoxal + H2O + O2
glyoxylate + H2O2
-
-
-
-
?
glyoxal + H2O + O2
glyoxylate + H2O2
-
-
-
-
?
glyoxylic acid + H2O + O2
?
-
12.4% activity compared to methylglyoxal
-
-
?
glyoxylic acid + H2O + O2
?
27% activity compared to methylglyoxal
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
-
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
100% activity
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
100% activity
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
-
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
100% activity
-
-
?
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2-oxopropanal + H2O + O2
pyruvate + H2O2
glyoxal + H2O + O2
glyoxylate + H2O2
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
2-oxopropanal + H2O + O2
pyruvate + H2O2
-
-
-
-
?
2-oxopropanal + H2O + O2
pyruvate + H2O2
-
-
-
-
?
glyoxal + H2O + O2
glyoxylate + H2O2
-
-
-
-
?
glyoxal + H2O + O2
glyoxylate + H2O2
-
-
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
-
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
-
-
-
?
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additional information
-
no activation is observed with Mg2+, Zn2+, Fe2+, or Mn2+
Cu2+
-
0.7-0.8 equivalents of Cu2+ per mol enzyme
Cu2+
-
full activation takes more than 1 h with 1 mM CuSO4 at pH 6.0
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phosphate
-
millimolar inhibitor
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additional information
-
purified native glyoxal oxidase is catalytically inactive, but can be oxidatively activated by lignin peroxidase molybdicyanide (K3Mo(CN)8) or hexachloroiridate (Na2IrCl6), or Mn3+ EDTA
-
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0.64
methylglyoxal
-
at pH 4.5 and 25°C
1.3
methylglyoxal
-
at pH 4.5 and 25°C
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198
methylglyoxal
-
at pH 4.5 and 25°C
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1
phosphate
-
at pH 6.0, temperature not specified in the publication
5.1
phosphate
-
at pH 4.5, temperature not specified in the publication
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4 - 6
-
more than 30% activity at pH 4.0 and 6.0, no activity at pH 3.0 and above pH 7.0
4.5 - 6
-
glyoxal oxidase activity is approximately 50% of its maximum at pH 4.5
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20 - 50
-
about 35% activity at 20°C, 100% activity at 30°C, about 95% activity at 40°C, and about 40% activity at 50°C. Less than 20% activity between 60 and 80°C
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4.7
-
isoelectric focusing
4.9
-
isoelectric focusing
5.1
-
isoelectric focusing
5.1
-
calculated from amino acid sequence
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-
UniProt
brenda
-
UniProt
brenda
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GLOX_PHACH
559
0
59168
Swiss-Prot
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57000
-
x * 57000, calculated from amino acid sequence
68000
-
1 * 68000, SDS-PAGE
70000
-
x * 70000, SDS-PAGE
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?
-
x * 70000, SDS-PAGE
?
-
x * 57000, calculated from amino acid sequence
?
-
x * 57000, calculated from amino acid sequence; x * 70000, SDS-PAGE
-
monomer
-
1 * 68000, SDS-PAGE
monomer
-
1 * 68000, SDS-PAGE
-
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glycoprotein
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five potential N-glycosylation sites (Asn-Xaa-Ser/Thr) are indicated at Asn11, Asn24, Asn78, Asn209, and Asn399
glycoprotein
-
five potential N-glycosylation sites (Asn-Xaa-Ser/Thr) are indicated at Asn11, Asn24, Asn78, Asn209, and Asn399
-
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DEAE Bio-Gel A column chromatography
-
Ni2+-Histag column chromatography, and gel filtration
-
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expressed in Aspergillus nidulans
-
expressed in Pichia pastoris strain GS115
-
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Kersten, P.J.; Kirk, T.K.
Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium
J. Bacteriol.
169
2195-2201
1987
Phanerochaete chrysosporium (Q01772)
brenda
Kersten, P.J.; Witek, C.; vanden Wymelenberg, A.; Cullen, D.
Phanerochaete chrysosporium glyoxal oxidase is encoded by two allelic variants: structure, genomic organization, and heterologous expression of glx1 and glx2
J. Bacteriol.
177
6106-6110
1995
Phanerochaete chrysosporium (Q01772), Phanerochaete chrysosporium BKM-F-1767 (Q01772)
brenda
Whittaker, M.M.; Kersten P.J.; Nakamura, N.; Sanders-Loehr, J.; Schweizer, E.S.; Whittaker, J.W.
Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase
J. Biol. Chem.
271
681-687
1996
Phanerochaete chrysosporium (Q01772)
brenda
Son, Y.L.; Kim, H.Y.; Thiyagarajan, S.; Xu, J.J.; Park, S.M.
Heterologous expression of Phanerochaete chrysoporium glyoxal oxidase and its application for the coupled reaction with manganese peroxidase to decolorize malachite green
Mycobiology
40
258-262
2012
Phanerochaete chrysosporium (Q01772), Phanerochaete chrysosporium BKM-F-1767 (Q01772)
brenda
Kersten, P.J.
Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase
Proc. Natl. Acad. Sci. USA
87
2936-2940
1990
Phanerochaete chrysosporium (Q01772), Phanerochaete chrysosporium BKM-F-1767 (Q01772)
brenda
Kersten, P.J; Cullen, D.
Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium
Proc. Natl. Acad. Sci. USA
90
7411-7413
1993
Phanerochaete chrysosporium (Q01772), Phanerochaete chrysosporium BKM-F-1767 (Q01772)
brenda
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