Information on EC 1.2.3.15 - (methyl)glyoxal oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Phanerochaete chrysosporium

EC NUMBER
COMMENTARY hide
1.2.3.15
-
RECOMMENDED NAME
GeneOntology No.
(methyl)glyoxal oxidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxopropanal + H2O + O2 = pyruvate + H2O2
show the reaction diagram
(2)
-
-
-
glyoxal + H2O + O2 = glyoxylate + H2O2
show the reaction diagram
(1)
-
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxopropanal + H2O + O2
pyruvate + H2O2
show the reaction diagram
acetaldehyde + H2O + O2
?
show the reaction diagram
acetaldehyde + H2O + O2
acetate + H2O2
show the reaction diagram
61% activity compared to methylglyoxal
-
-
?
acetol + H2O + O2
?
show the reaction diagram
4% activity compared to methylglyoxal
-
-
?
dihydroxyacetone + H2O + O2
?
show the reaction diagram
DL-glyceraldehyde + H2O + O2
?
show the reaction diagram
formaldehyde + H2O + O2
?
show the reaction diagram
-
3.6% activity compared to methylglyoxal
-
-
?
formaldehyde + H2O + O2
formate + H2O2
show the reaction diagram
54% activity compared to methylglyoxal
-
-
?
glycolaldehyde + H2O + O2
?
show the reaction diagram
-
8.1% activity compared to methylglyoxal
-
-
?
glycolaldehyde + H2O + O2
hydroxyacetate + H2O2
show the reaction diagram
69% activity compared to methylglyoxal
-
-
?
glyoxal + H2O + O2
?
show the reaction diagram
glyoxal + H2O + O2
glyoxylate + H2O2
show the reaction diagram
glyoxylic acid + H2O + O2
?
show the reaction diagram
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
show the reaction diagram
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxopropanal + H2O + O2
pyruvate + H2O2
show the reaction diagram
glyoxal + H2O + O2
glyoxylate + H2O2
show the reaction diagram
methylglyoxal + H2O + O2
methylglyoxylate + H2O2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation is observed with Mg2+, Zn2+, Fe2+, or Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
millimolar inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.64 - 1.3
methylglyoxal
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
198
methylglyoxal
Phanerochaete chrysosporium
-
at pH 4.5 and 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 5.1
phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
about 35% activity at 20C, 100% activity at 30C, about 95% activity at 40C, and about 40% activity at 50C. Less than 20% activity between 60 and 80C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
isoelectric focusing
4.9
-
isoelectric focusing
5
-
isoelectric focusing
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Bio-Gel A column chromatography
-
Ni2+-Histag column chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus nidulans
-
expressed in Pichia pastoris strain GS115
-