Information on EC 1.2.3.4 - oxalate oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
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: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.2.3.4
-
RECOMMENDED NAME
GeneOntology No.
oxalate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
show the reaction diagram
-
-
-
-
oxalate + O2 + 2 H+ = 2 CO2 + H2O2
show the reaction diagram
The computer model supports the following reaction mechanism: The Oxo-Mn(2)-oxalate complex exists as a mixture of five-and six-coordinate species. The form with coordinatively unsaturated Mn(2) site reacts with dioxygen on the quartet potential energy surface. In this step, the proton from oxalate monoanion is transferred to dioxygen through the first-shell glutamate. The proton-transfer triggers the C-C bond cleavage, and the electron follows the proton. Simultaneously, the second electron, necessary to produce the peroxo species, is provided by manganese. This step, which is also rate-limiting, yields the first CO2 molecule and the reactive intermediate in which the formyl radical anion coordinates the high-spin Mn(3). The quartet to sextet spin transition, which involves a small apparent barrier, allows for the formyl radical -> Mn(3) electron transfer. This step leads to the product-active site complex, which upon protonation decays to H2O2, CO2, and the active site is then ready to begin the next catalytic cycle
-
PATHWAY
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
-
oxalate degradation IV
-
SYSTEMATIC NAME
IUBMB Comments
oxalate:oxygen oxidoreductase
Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had been thought [3].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aero-oxalo dehydrogenase
-
-
-
-
Germin
-
-
-
-
Germin
-
-
Germin
-
-
Germin
-
-
Germin
P15290
-
Germin GF-2.8
-
-
-
-
Germin GF-3.8
-
-
-
-
germin-like oxidase
-
-
HvOxo1
-
-
oxalate oxidase
-
-
oxalate oxidase
-
-
oxalate oxidase
-
-
oxalate oxidase
P15290
-
oxalate: O2 oxidoreductase
-
-
oxalate: O2 oxidoreductase
Hordeum vulgare BH393
-
-
-
oxalate:oxygen oxidoreductase
-
-
oxalic acid oxidase
-
-
-
-
OXO
P45850
-
OXO
Hordeum vulgare BH393
-
-
-
OXO-G
Q5ZH56
G-isoform
CAS REGISTRY NUMBER
COMMENTARY
9031-79-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
oat, with freshly sliced oat radicles little oxalate degradation is oberserved
-
-
Manually annotated by BRENDA team
ATCC 90466, oxalate oxidase allelic isoforms C and G
-
-
Manually annotated by BRENDA team
strain FP-10572
-
-
Manually annotated by BRENDA team
Ceriporiopsis subvermispora FP-10572
strain FP-10572
-
-
Manually annotated by BRENDA team
barley
UniProt
Manually annotated by BRENDA team
barley, var. Alpaca, freshly sliced barley radicles are less effective in oxalate degradation than rye radicles
-
-
Manually annotated by BRENDA team
computer model of the reaction mechanism
-
-
Manually annotated by BRENDA team
strain pallas, P-01, P-02
-
-
Manually annotated by BRENDA team
transgenic potato plantlets expressing the barley oxalate oxidase enzyme, show a relatively higher salinity tolerance than the non-transgenic genotypes in vitro, but in the glasshouse the results are less consistent
-
-
Manually annotated by BRENDA team
Hordeum vulgare BH393
-
-
-
Manually annotated by BRENDA team
banana
-
-
Manually annotated by BRENDA team
cultivar Xiangnuo 1
-
-
Manually annotated by BRENDA team
cultivars PI 255956, PI 535278 (Tars-046A) and cv. Wolven Pole, oxalate concentration in infected (infected with Sclerotinia sclerotiorum) stems of Wolven Pole is higher than in PI 255956 and PI535278. Inoculated stems of Wolven Pole have oxalate oxidase, the Sclerotinia sclerotorum resistent lines PI 255959 and PI 535278 not. Phaseolus coccineus is not as oxalat sensitiv as Phaseolus vulgaris. Infection of Phaseolus coccineus with Sclerotinia scerotorum increased the levels of oxalate, with the highest concentration in Woven Pole
-
-
Manually annotated by BRENDA team
cvs. Huron (navy), Othello (pinto) and Newport (navy), Phaseolus vulgaris is more oxalate sensitive than Phaseolus coccineus, with Othello being the most sensitive, Huron the most tolerant, and Newport intermediate. Huron is more resistant to Sclerotinia sclerotiorum than the other two cultivars
-
-
Manually annotated by BRENDA team
strain OX-53
-
-
Manually annotated by BRENDA team
Pseudomonas sp. OX-53
strain OX-53
-
-
Manually annotated by BRENDA team
commercial blend
-
-
Manually annotated by BRENDA team
hybrid, var CSH-14
-
-
Manually annotated by BRENDA team
line CSH-14
-
-
Manually annotated by BRENDA team
variant CSH-14
-
-
Manually annotated by BRENDA team
variant KH-105
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
Sorghum sp.
strain CSH-5
-
-
Manually annotated by BRENDA team
Sorghum sp. CSH-5
strain CSH-5
-
-
Manually annotated by BRENDA team
common wheat
-
-
Manually annotated by BRENDA team
cultivar Daichino-Minori
-
-
Manually annotated by BRENDA team
wheat, var.Zentos, freshly sliced wheat radicles are less effective in oxalate degradation than rye radicles
-
-
Manually annotated by BRENDA team
commercial blend, freshly sliced spelt radicles are less effective in oxalate degradation than rye radicles
-
-
Manually annotated by BRENDA team
maize, with maize radicle negligble oxalate degradation is observed
-
-
Manually annotated by BRENDA team
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
FMN, FAD, NAD+, and riboflavin at 1 mM in the presence of nanoparticles have practically no effect on native and immobilized enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.7
-
oxalate
-
oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25C)
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.9
-
acetate
-
in citrate buffer, at pH 4.0 and 22C
28
-
glycolate
-
in citrate buffer, at pH 4.0 and 22C
15
-
glyoxylate
-
in citrate buffer, at pH 4.0 and 22C
52
-
malate
-
in citrate buffer, at pH 4.0 and 22C
3
-
malonate
-
in citrate buffer, at pH 4.0 and 22C
17
-
pyruvate
-
in citrate buffer, at pH 4.0 and 22C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
4.5
-
20% activity at pH 2.0 and 4.5
2.5
4.5
-
30% activity at pH 2.5 and 4.5
2.5
4.5
-
60% activity at pH 2.5 and 4.5
2.5
6
-
the catalytic efficiency (Vmax/Km) increases continuously to lower pH
3.5
5.5
-
about 57% activity at pH 3.5, 100% activity at pH 4.0, about 82% activity at pH 4.5, about 60% activity at pH 5.0, about 27% activity at pH 5.5
4
7
Sorghum sp.
-
50% activity at pH 4.0 and 7.0
4.5
7
-
approx. 50% of maximal activity at pH 5.0 and pH 7.0, respectively, polyvinyl alcohol membrane immobilized oxalate oxidase
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
55
-
in situ, max. oxalate degradation in the liquid phase of a spinach (commercial frozen) preparation, the rate of oxalate degradation in spinach suspension and the solid phase is lower. In fresh spinach (without any heat treatment) little oxalate degradation occurs
20
70
-
in situ in an oxalate solution at different time intervals of incubation
25
50
-
50% activity at 25C and 50C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilized on alkylamine glass
-
after 90 min treatment with trypsin 10% activity retained by free protein, 35% activity retained by immobilized protein on PEG1900 and 30% activity retained by immobilized protein on PEG5000
-
immobilized on PEG1900 and PEG5000
-
enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate (SDS)
-
based on the absoption changes at 325 nm, it is possible to estimate the half-life of the Mn5+ species at room temperature: t1/2 = 42 h (pH 4) or 95 h (pH 7)
-
immobilized on zirkonia coated alkylamine glass, retains 97% of enzyme activity
-
the immobilized enzyme on modified mica chip retains 65.35% of the specific activity of free enzyme
-
the polyvinyl chloride-immobilized enzyme retains 65% of specific activity of free enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by treatment with K3Fe(CN)6 decreases activity, desalting restores initial activity
-
288378
resistant against Na2IrCl6
-
288378