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Enzyme Nomenclature
Information on EC 1.2.3.15 - (methyl)glyoxal oxidase
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1.2.3.15 (methyl)glyoxal oxidaseIUBMB Comments
The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GLOX
GLX
Glx1
GLX2
methylglyoxal oxidase
Glx1
-
-
-
-
GLX2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxopropanal + H2O + O2 = pyruvate + H2O2
(2)
-
-
-
glyoxal + H2O + O2 = glyoxylate + H2O2
(1)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(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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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
acetaldehyde + H2O + O2
acetate + H2O2
61% activity compared to methylglyoxal
-
-
?
acetol + H2O + O2
?
4% activity compared to methylglyoxal
-
-
?
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
-
-
?
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
-
-
-
?
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
?
45% activity compared to methylglyoxal
-
-
?
glyoxal + H2O + O2
?
3.3% activity compared to methylglyoxal
-
-
?
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
-
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
100% activity
-
-
?
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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-oxopropanal + H2O + O2
pyruvate + H2O2
-
-
-
?
glyoxal + H2O + O2
glyoxylate + H2O2
-
-
-
?
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
additional information
no activation is observed with Mg2+, Zn2+, Fe2+, or Mn2+
Cu2+
full activation takes more than 1 h with 1 mM CuSO4 at pH 6.0
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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). A0A5B7AQ80_DAVIN
549
0
60315
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5B7AWU1_DAVIN
374
1
40752
TrEMBL
other Location (Reliability: 3)
A0A060SXH6_PYCCI
558
0
59658
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7C6G1_DAVIN
281
0
31036
TrEMBL
other Location (Reliability: 2)
A0A5B7APE5_DAVIN
554
1
60973
TrEMBL
Secretory Pathway (Reliability: 5)
A0A5B7BK86_DAVIN
536
0
58568
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7C570_DAVIN
310
1
35465
TrEMBL
other Location (Reliability: 1)
GLOX_PHACH
559
0
59168
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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