Information on EC 1.1.3.15 - (S)-2-hydroxy-acid 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: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.1.3.15
-
RECOMMENDED NAME
GeneOntology No.
(S)-2-hydroxy-acid oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
show the reaction diagram
A flavoprotein, FMN. Exists as two major isoenzymes. The A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase. The B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as L-amino acid oxidase, EC 1.4.3.2
-
-
-
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
show the reaction diagram
the catalytic residue is Phe23, reaction mechanism
Q07523
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
show the reaction diagram
the pH affects the kinetic steps of the catalytic mechanism of human glycolate oxidase, the enzyme shows a ping-pong bi-bi kinetic mechanism between pH 6.0 and 10.0, overview. Formation of the enzyme-substrate complex suggests the presence of a protonated group participating in substrate binding
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Glyoxylate and dicarboxylate metabolism
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxy-acid:oxygen 2-oxidoreductase
A flavoprotein (FMN). Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as EC 1.4.3.2, L-amino-acid oxidase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(S)-2-hydroxy-acid oxidase, peroxisomal
-
-
-
-
2-hydroxy acid oxidase
-
3 isoenzymes: HAOX1, HAOX2, HAOX3
glycolate oxidase
-
-
-
-
glycolate oxidase
-
-
glycolate oxidase
Q56ZN0
-
glycolate oxidase
-
-
glycolate oxidase
-
-
glycolate oxidase
Q9UJM8
-
glycolate oxidase
-
-
glycolate oxidase
-
-
glycolate oxidase
Q19U05
-
glycolate oxidase
Pseudomonas stutzeri, Roseobacter sp.
-
-
glycolate oxidase
-
-
glycolate oxidase
-
-
GOX
-
-
-
-
Hao2
-
-
HAOX1
-
-
-
-
HAOX2
-
-
-
-
HAOX3
-
-
-
-
hydroxy-acid oxidase A
-
-
-
-
hydroxy-acid oxidase B
-
-
-
-
hydroxyacid oxidase A
-
-
-
-
L-2-hydroxy acid oxidase
-
-
-
-
L-2-hydroxy acid oxidase
-
-
L-2-hydroxyacid oxidase A
-
-
L-alpha-hydroxy acid oxidase
-
-
-
-
L-amino acid oxidase
-
-
L-LAC-OX
-
-
L-lactate monooxygenase
-
-
L-lactate oxidase
Pediococcus sp.
-
-
L-lactate oxidase
-
-
L-LOx
Pediococcus sp.
-
-
lactate oxidase
Q9CG58
-
lactate oxidase
Lactococcus lactis IL 1403
Q9CG58
-
-
lactate oxidase
Pediococcus sp.
-
-
lactate oxidase
A9QH69, A9QH71
flavin mononucleotide-dependent
lactate oxidase
Streptococcus iniae QMA0177
A9QH71
flavin mononucleotide-dependent
-
LctO
Lactococcus lactis IL 1403
Q9CG58
-
-
LctO
Pediococcus sp.
-
-
LctO
A9QH69
type 1 enzyme
LctO
A9QH71
type 2 enzyme (novel variant of lactate oxidase gene)
LctO
Streptococcus iniae QMA0177
A9QH71
type 2 enzyme (novel variant of lactate oxidase gene)
-
long chain hydroxy acid oxidase
-
-
long chain l-2-hydroxy acid oxidase
-
-
long chain L-2-hydroxy acid oxidase 2
-
-
LOX
Pediococcus sp.
-
-
oxidase, L-2-hydroxy acid
-
-
-
-
additional information
-
the enzyme belongs to the FMN-dependent enzyme family
CAS REGISTRY NUMBER
COMMENTARY
9037-63-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 11563
-
-
Manually annotated by BRENDA team
green amaranth
-
-
Manually annotated by BRENDA team
strain DSM 10452
-
-
Manually annotated by BRENDA team
cv. Pripyat, various isozymes
-
-
Manually annotated by BRENDA team
authors suggest a different annotation for the lctO gene with LctO translation starting at Met-18, encoding a protein of 366 amino acids
UniProt
Manually annotated by BRENDA team
IL 1403
UniProt
Manually annotated by BRENDA team
Lactococcus lactis IL 1403
IL 1403
UniProt
Manually annotated by BRENDA team
correlation of enzyme activity with content of beta-N-oxalyl-L-alpha,beta-diaminopropionic acid under high light treatment
-
-
Manually annotated by BRENDA team
cv. Shishoubaimao
Uniprot
Manually annotated by BRENDA team
Pediococcus sp.
-
-
-
Manually annotated by BRENDA team
Pediococcus sp.
commercial preparation
-
-
Manually annotated by BRENDA team
plant
-
-
-
Manually annotated by BRENDA team
suffering chronic dietary iron overload
-
-
Manually annotated by BRENDA team
Roseobacter sp.
gene glcD
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
strains QMA0165 (type 1 enzyme)
UniProt
Manually annotated by BRENDA team
type 2 lactate oxidase isolated from Strptococcus iniae; strain QMA0177 (novel type 2 enzyme), major pathogen of farmed fish, type 2 is an isolate from diseased barramundi (Lates calcarifer) in Northern Territory, Australia
UniProt
Manually annotated by BRENDA team
Streptococcus iniae QMA0177
type 2 lactate oxidase isolated from Strptococcus iniae; strain QMA0177 (novel type 2 enzyme), major pathogen of farmed fish, type 2 is an isolate from diseased barramundi (Lates calcarifer) in Northern Territory, Australia
UniProt
Manually annotated by BRENDA team
activities of both lactarte oxidase and pyruvate oxidase in wild-type cultures are detectable even in the early exponential phase of growth and attain the highest levels in the early stationary phase
-
-
Manually annotated by BRENDA team
cv. Voronezhskaya 76, various isozymes
-
-
Manually annotated by BRENDA team
gene GO1
-
-
Manually annotated by BRENDA team
mesophyll and bundle sheath isoforms
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme is a member of the flavoenzyme family
malfunction
-
the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
metabolism
Q56ZN0
the enzyme is involved in the glyoxylate metabolism, overview
metabolism
-
the enzyme is involved in the metabolism of glycolate
metabolism
-
the enzyme is involved in the metabolism of glycolate, glycolate oxidase is a key enzyme involved in C3 photorespiration metabolic pathway, the process where plants lose up to half of assimilated carbon
metabolism
-
inactivation of gene pox encoding pyruvate oxidase causes a dramatic reduction in H2O2 production from lactate, suggesting a synergistic action of the two oxidases in converting lactate into H2O2. The pox mutant of Streptomyces oligofermentans fails to inhibit Streptomyces mutans even though lox is active
physiological function
-, Q10CE4
a positive and linear correlation exists between GLO activities and the net photosynthetic rates, PN, and photoinhibition subsequently occurrs once PN reduction surpasses 60%, indicating GLO can exert a strong regulation over photosynthesis. Isocitrate lyase and malate synthase, two key enzymes in the glyoxylate cycle, are highly up-regulated under GLO deficiency
physiological function
-
the enzyme performs an essential step in the operation of the oxidative photorespiratory cycle accompanying photosynthetic CO2 assimilation in C3 plants
physiological function
-
role in C3 and C4 plants and associated regulation mechanisms
physiological function
-
pharmacological role of the enzyme in the management of blood pressure
physiological function
-
H2O2 production, especially lactate oxidase, allows Streptomyces oligofermentans to out-compete Streptomyces mutans in oral commensals, the enzyme mainly contributes to H2O2 production in stationary phase. But lactate oxidase requires cofunction of pyruvate oxidase for successfully inhibiting Streptomyces mutans
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
-
glucose-repressible lactate oxidase is likely responsible for H2O2 production
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
no decarboxylation
-
?
2-hydroxy-3-methylvalerate + O2
?
show the reaction diagram
-
A95G-mutant
-
-
?
2-hydroxybutanoate + bromopyruvate + ?
bromolactate + pyruvate + ?
show the reaction diagram
-
transhydrogenation reaction
-
?
2-hydroxybutyrate + O2
?
show the reaction diagram
-
wild-type and A95G-mutant
-
-
?
2-hydroxyisovalerate + O2
?
show the reaction diagram
-
A95G-mutant
-
-
?
2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxo-octanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Q9UJM8
-
-
-
r
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
show the reaction diagram
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
show the reaction diagram
-
substrates for isoenzymes HAOX1, HAOX2
-
?
2-hydroxyvalerate + O2
?
show the reaction diagram
-
wild-type and A95G-mutant
-
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
48% of the activity compared to glycolate
-
?
D-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
traces of activity
-
?
DL-2-hydroxy-3-butynoate + O2
2-oxo-3-butynoate + H2O2
show the reaction diagram
-
good substrate, but inactivation after 25 turnovers
-
?
DL-2-hydroxy-3-heptynoate + O2
2-oxo-3-heptynoate + H2O2
show the reaction diagram
-
86% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-hexynoate + O2
2-oxo-3-hexynoate + H2O2
show the reaction diagram
-
65% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
show the reaction diagram
-
70% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-pentynoate + O2
2-oxo-3-pentynoate + H2O2
show the reaction diagram
-
2fold higher activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-4-methylmercaptobutyrate + 2,6-dichlorophenolindophenol
2-oxo-4-methylmercaptobutyrate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
good substrate for long chain oxidase, low activity for short chain oxidase
-
?
DL-2-hydroxy-4-methylthiobutanoic acid + 2,6-dichlorophenolindophenol
2-oxo-4-methylthiobutanoic acid + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + 2,4-dinitrophenyl hydrazone
2-oxobutyrate + ?
show the reaction diagram
-
low activity
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
low activity for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
higher affinity with C5 and C6 hydroxy acids
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
68% of the activity compared to glycolate
-
?
DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol
2-oxocaproate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxydecanoate + 2,6-dichlorophenolindophenol
2-oxodecanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
good substrate for long chain oxidase, traces of activity for short chain oxidase
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyisovalerate + 2,4-dinitrophenyl hydrazone
2-oxoisovalerate + ?
show the reaction diagram
-
very low activity
-
?
DL-2-hydroxyisovalerate + 2,6-dichlorophenolindophenol
2-oxoisovalerate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
no activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxooctanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol
2-oxovalerate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
39% of the activity compared to glycolate
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
show the reaction diagram
-
best substrate tested
-
?
DL-3-indolelactate + 2,6-dichlorophenolindophenol
3-indolepyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-3-indolelactate + O2
3-indolepyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-3-methoxy-4-hydroxymandelate + 2,6-dichlorophenolindophenol
(3-methoxy-4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
DL-beta-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
no activity for short chain oxidase
-
?
DL-glycerate + O2
? + H2O2
show the reaction diagram
-
-
-
?
DL-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
low activity
-
?
DL-mandelate + O2
phenylglyoxylic acid + H2O2
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-methionine + O2
? + H2O2
show the reaction diagram
-
-
-
?
DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol
(4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
no activity for short chain oxidase
-
?
DL-p-hydroxymandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
show the reaction diagram
-
90% of the activity compared to DL-2-hydroxybutyrate
-
?
glycerate + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + 2,4-dinitrophenyl hydrazone
glyoxylate + ?
show the reaction diagram
-
best substrate tested
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Q9UJM8
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
highest activity for short chain oxidase, no activity for long chain oxidase
-
?
glycolate + ferricyanide
glyoxylate + ferrocyanide
show the reaction diagram
-
-
-
?
glycolate + ferricyanide
glyoxylate + ferrocyanide
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-, Q10CE4
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
plant
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
Q56ZN0
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
the catalytic adduct is formed by hydrogen abstraction from the re-face of glycolate
-
-
?
glyoxalate + O2
oxalate + H2O2
show the reaction diagram
-
-
-
-
?
glyoxylate + 2,4-dinitrophenyl hydrazone
oxalate + ?
show the reaction diagram
-
25% of the activity compared to glycolate
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Q9UJM8
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
-
-
-
?
glyoxylate + ferricyanide
? + ferrocyanide
show the reaction diagram
-
-
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
-
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
-
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
40% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
substrate for isoenzyme HAOX1
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
26% of the activity compared to glycolate
-
?
glyoxylate thiohemiacetals + O2
? + H2O2
show the reaction diagram
-
possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
-
?
homoserine + O2
? + H2O2
show the reaction diagram
-
traces of activity
-
?
L-2-hydroxy octanoate + O2
2-oxo-octanoate + H2O2
show the reaction diagram
Q07523
-
-
-
?
L-2-hydroxy palmitate + O2
2-oxo-palmitate + H2O2
show the reaction diagram
Q07523
-
-
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-methyl-thiopropionate + HCO3- + H+
show the reaction diagram
-
oxidative decarboxylation
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
-
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
no activity for short chain oxidase
-
?
L-2-hydroxyisocaproate + 2,4-dinitrophenyl hydrazone
2-oxoisocaproate + ?
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
substrate for isoenzyme B
-
?
L-2-hydroxyphenyllactate + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyphenyllactate + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-4-chloromandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-fluoromandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methoxymandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methylmandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-nitromandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-trifluoromethylmandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-alanine + O2
? + H2O2
show the reaction diagram
-
low activity
-
?
L-isoleucine + O2
? + H2O2
show the reaction diagram
-
low activity
-
?
L-lactate + 2,4-dinitrophenyl hydrazone
pyruvate + ?
show the reaction diagram
-
very low activity
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
very low activity
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
lower activity for preparation from "heavy" mitochondria
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
Q07523
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
high activity, does not act on D-lactate
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
Pediococcus sp.
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-leucine + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
L-leucine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-leucine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-leucine + O2
? + H2O2
show the reaction diagram
-
highest activity
-
?
L-lysine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
-
-
-
?
L-mandelate + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-mandelate + O2
?
show the reaction diagram
-
A95G-mutant is also reactive
-
-
?
L-mandelate + O2
?
show the reaction diagram
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-methionine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-methionine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-phenylalanine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
-
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
L-tryptophan + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tryptophan + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tryptophan + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tyrosine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-valine + O2
? + H2O2
show the reaction diagram
-
low activity
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Q9CG58
-
-
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
A9QH69, A9QH71
-
-
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Pediococcus sp.
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Lactococcus lactis IL 1403
Q9CG58
-
-
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Streptococcus iniae QMA0177
A9QH71
-
-
-
?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
show the reaction diagram
-
may be the physiological substrates
-
?
mandelate + O2
phenylpyruvate + H2O2
show the reaction diagram
Q07523
oxidation of an L-2-hydroxy acid to a 2-oxoacid, model for the binding of L-mandelate into the active site, overview
-
-
?
additional information
?
-
-
interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
Q19U05
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
additional information
?
-
-
no substrate: oxalate, acetate, pyruvate, glycerol, propionate, succinate, fumarate, malate, maleate, tartrate, oxaloacetate, 2-oxoglutarate, glycocol,L-alanine, serine, glutamate, ascorbate, glucose, and fructose
-
-
-
additional information
?
-
-, Q10CE4
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
-
additional information
?
-
Streptococcus pneumoniae GTC13809
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
no decarboxylation
-
?
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
show the reaction diagram
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
show the reaction diagram
-
substrates for isoenzymes HAOX1, HAOX2
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
48% of the activity compared to glycolate
-
?
D-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
traces of activity
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
higher affinity with C5 and C6 hydroxy acids
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
show the reaction diagram
-
68% of the activity compared to glycolate
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
low activity
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
show the reaction diagram
-
39% of the activity compared to glycolate
-
?
DL-glycerate + O2
? + H2O2
show the reaction diagram
-
-
-
?
DL-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
DL-methionine + O2
? + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-, Q10CE4
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
plant
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
Q56ZN0
-
-
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
-
?
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
-
glycolate + O2
glyoxylate + H2O2
show the reaction diagram
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
-
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
-
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
40% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
substrate for isoenzyme HAOX1
-
?
glyoxylate + O2
? + H2O2
show the reaction diagram
-
26% of the activity compared to glycolate
-
?
glyoxylate thiohemiacetals + O2
? + H2O2
show the reaction diagram
-
possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
-
?
homoserine + O2
? + H2O2
show the reaction diagram
-
traces of activity
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-methyl-thiopropionate + HCO3- + H+
show the reaction diagram
-
oxidative decarboxylation
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
show the reaction diagram
-
substrate for isoenzyme B
-
?
L-alanine + O2
? + H2O2
show the reaction diagram
-
low activity
-
?
L-isoleucine + O2
? + H2O2
show the reaction diagram
-
low activity
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
-
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
high activity, does not act on D-lactate
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
show the reaction diagram
Pediococcus sp.
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-leucine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-leucine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-leucine + O2
? + H2O2
show the reaction diagram
-
highest activity
-
?
L-lysine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-mandelate + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-methionine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-methionine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-phenylalanine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tryptophan + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tryptophan + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tryptophan + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-tyrosine + O2
? + H2O2
show the reaction diagram
-
-
-
?
L-valine + O2
? + H2O2
show the reaction diagram
-
low activity
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Q9CG58
-
-
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
A9QH69, A9QH71
-
-
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Pediococcus sp.
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Lactococcus lactis IL 1403
Q9CG58
-
-
-
?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
show the reaction diagram
-
may be the physiological substrates
-
?
lactate + O2
pyruvate + H2O2
show the reaction diagram
Streptococcus iniae QMA0177
A9QH71
-
-
-
?
additional information
?
-
-
interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
Q19U05
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
additional information
?
-
-, Q10CE4
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
-
additional information
?
-
Streptococcus pneumoniae GTC13809
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
both FMN and FAD, with FAD 46.8% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 45.5% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 67% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 53.6% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 29% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 71.1% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 47.4% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 36.4% of the activty with FMN
FAD
-
both FMN and FAD, with FAD 51.7% of the activty with FMN
flavin
-
dependent on
FMN
-
most effective electron acceptor
FMN
-
three-residue insertion of loop 4 in isozyme beta2 influences ionisation state of FMN
FMN
Mammalia, plant
-
-
FMN
-
one FAD per subunit
FMN
-
one FAD per two subunits
FMN
-
2 mol FAD per mol enzyme
FMN
-
0.125 mol 5'-FMN per monomer, not covalently bound
FMN
-
both FMN and FAD, with FAD 46.8% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 45.5% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 67% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 53.6% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 29% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 71.1% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 47.7% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 36.4% of the activity with FMN
FMN
-
both FMN and FAD, with FAD 51.7% of the activity with FMN
FMN
Q19U05
the enzyme contains a GOX-like-riboflavin-5'-phosphate conserved domain
FMN
-
dependent on
additional information
-
evidence for a second, unknown chromophore
-
additional information
-
no activity with riboflavin and lumiflavin
-
additional information
Q9CG58
no cofactor: NAD+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
Q9CG58
up to 4fold induction
Cd2+
Q9CG58
induction
Cu2+
Q9CG58
exposure of cells to mM copper sulfate, strong induction. Highest induction at 0.3 mM, about 16-fold increase in activity. Identification of a copper-response element in the 5'-region of the LctO gene
CuSO4
Q9CG58
induces copper regulated promoter, upregulates LctO 17fold (2D gel)
additional information
Q9CG58
Zn2+, Fe2+, Ni2+, Mn2+, and Ca2+ have no significant effect on lctO expression
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(R)-lactate
-
at pH 7.0
2,6-dichlorophenolindophenol
-
inhibition by excess substrate
2-hydroxybutynoate
-
inhibition of transhydrogenation reaction
2-Hydroxybutyrate
-
long chain oxidase, 13-17% inhibition at 17 mM
2-Hydroxybutyrate
-
at pH 7.0
2-oxobutyrate
-
non-competitive inhibition at 5 mM
2-oxoisocaproate
-
non-competitive inhibition at 5 mM, most active inhibitor of 2-keto acids, oxidation of 2-hydroxybutyrate most sensitive
2-oxoisovalerate
-
non-competitive inhibition at 5 mM
2-oxovalerate
-
non-competitive inhibition at 5 mM
2-pyridylhydroxymethanesulfonate
-
strong inhibition between 0.1-1 mM
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-decyl-2,5-dioxo-4-hydroxy-3-pyrroline
-
bound to the active site in the three-dimensional structure
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
35% inhibition at 0.010 mM
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole
-
bound to the active site in the three-dimensional structure
4-carboxy-5-dodecylsulfanyl-1,2,3-triazole
-
-
4-chloromercuribenzoate
-
strong inhibition at 0.01 mM
4-chloromercuribenzoate
-
long chain oxidase, 29-42% inhibition at 0.001 mM, short chain oxidase: 70-75% inhibition at 0.001 mM
4-chloromercuribenzoate
-
inhibition at 50 mM
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
8-hydroxyquinoline
-
50% inhibition at 0.05 mM
8-hydroxyquinoline
-
5-17% inhibition at 1 mM
8-hydroxyquinoline
-
8-17% inhibition at 1 mM
acetate
-
mixed-type non-competitive inhibition
acetate
-
-
arsenate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
Atebrin
-
long chain oxidase, 72-76% inhibition at 1 mM, short chain oxidase: 68-76% inhibition at 1 mM
benzaldehyde
-
50% inhibition at 2 mM
Bipyridine
-
strong inhibition
Butyrate
-
-
Caproate
-
mixed-type non-competitive inhibition
chloride
-
inhibits the enzyme at high concentrations
Cibacron blue 3GA
-
at a concentration higher than 0.001 mM is a normal competitive inhibitor, at concentrations below 0.001 mM the inhibition is time-, dye- and pH-dependent
Cu2+
-
nearly complete inhibition at 0.025 mM
Cu2+
-
complete inhibition at 0.025 mM
Cu2+
-
short chain oxidase: 86% inhibition at 0.1 mM
Cu2+
-
50% inhibition at 0.2 mM
cysteine
-
28-38% inhibition of glycolate oxidation at 1 mM
diethyldithiocarbamate
-
competitive inhibition
diethyldithiocarbamate
-
51-55% inhibition at 1 mM
dihydrolipoate
-
competitive inhibition of 2-hydroxybutyrate oxidation
diphenylglycolic acid
-
11-17% inhibition at 52 mM
diphenylglycolic acid
-
50% inhibition at 52 mM, competitive
Dithionite
-
reduction of FMN
DL-2-hydroxy-3-butynoate
-
irreversible inactivation after 25 turnovers, covalent addition to the coenzyme
DL-2-hydroxy-3-heptynoate
-
inactivation after18000 turnovers
DL-2-hydroxy-3-hexynoate
-
inactivation after 8500 turnovers
DL-2-hydroxy-3-octynoate
-
inactivation after 15000 turnovers
DL-2-hydroxy-3-pentynoate
-
inactivation after 4800 turnovers
DL-2-hydroxyisocaproate
-
marked inhibition above 50 mM
DL-2-hydroxyvalerate
-
marked inhibition above 50 mM
DL-beta-Phenyllactate
-
short chain oxidase: 10% inhibition of glycolate oxidation, 81% inhibition of L-2-hydroxisocaproate oxidation at 10 mM
DL-Lipoate
-
long chain oxidase, 35% inhibition at 0.24 mM, short chain oxidase: 46-52% inhibition at 0.01 mM
DL-vinylglycolate
-
slight inactivation after 10000 turnovers
glycolate
-
inhibition above 1.7 mM
glycolate
-
inhibition by excess substrate
glyoxylate
-
inhibition by excess substrate
glyoxylate
-
substrate inhibition at concentrations above 4 mM
Heptanoate
-
-
Hexanoate
-
-
hydoxylamine
-
66-67% inhibition at 5 mM
hydroxylamine
-
50% inhibition at 5 mM, competitive
iodoacetamide
-
inhibition at 50 mM
iodoacetate
-
long chain oxidase, 31-36% inhibition at 0.1 mM, short chain oxidase: no inhibition
iodoacetate
-
inhibition at 50 mM
KCN
-
mixed-type inhibitor
KCN
-
30% inhibition of L-2-hydroxyisocaproate oxidation at 1 mM, 91% inhibition of glycolate oxidation at 1 mM
L-leucine
-
competitive inhibition
L-leucine
-
9-12% inhibition at 33 mM
L-Mandelate
-
at pH 7.0
L-Mandelate
-
inhibition by excess substrate
L-phenylalanine
-
long chain oxidase, 43% inhibition at 33 mM
malonate
-
-
NAD+
-
competitive
o-Iodosobenzoate
-
46-62% inhibition at 0.1 mM
o-Iodosobenzoate
-
46% inhibition at 0.1 mM
o-Iodosobenzoate
-
long chain oxidase, 95-100% inhibition at 0.1 mM, short chain oxidase: no inhibition
o-phenanthroline
-
strong inhibition between 0.1-1.0 mM
o-phenanthroline
-
5-23% inhibition at 1 mM
o-phenanthroline
-
5-14% inhibition at 1 mM
oxalate
-
mixed-type non-competitive inhibition, increasing inhibitory effects as the number of carbons in aliphatic chains decreases
oxalate
-
competitive inhibition
oxalate
-
18% inhibition of glycolate oxidation, 71% inhibition of glyoxylate oxidation at 0.03 mM
oxalate
-
-
oxalate
-
at pH 7.0
oxalate
-
34% inhibition at 5 mM, competitive
Oxamate
-
mixed-type non-competitive inhibition
phosphate
-
50% inhibition at 0.1 M
phosphate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
Propionate
-
mixed-type non-competitive inhibition
Propionate
-
-
pyruvate
-
competitive inhibition
pyruvate
-
26% inhibition at 5 mM
Quinacrine
-
6% inhibition at 1 mM
rotenone
-
50% inhibition at 0.1 mM
sodium sulfite
-
reduces FMN
succinate
-
-
succinate
-
mesophyll isoform
trans-Cinnamate
-
competitive inhibition
valerate
-
-
Mandelate
-
-
additional information
-
treatment with 4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid or 4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid results in a significant reduction or attenuation of blood pressure in an established or developing model of hypertension, deoxycorticosterone acetate-treated rats
-
additional information
-
development of selective inhibitors of Hao2 from screening of a compound library, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
arsenate
-
increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
ascorbate
-
17.5-26% activation at 1 mM
CuSO4
Q9CG58
200 microM for 45 min induces copper regulated promoter
EDTA
-
slight activation for short and long chain oxidases
Isocitrate
-
strong, bundle sheath isoform, slight, mesophyll isoform
phosphate
-
increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
succinate
-
strong, bundle sheath isoform
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0052
-
(S)-Lactate
-
pH 7.4, 25C
0.157
-
(S)-Lactate
-
at pH 7
0.175
-
(S)-Lactate
-
-
0.529
-
(S)-Lactate
-
25C, wild-type enzyme
0.863
-
(S)-Lactate
-
35C, wild-type enzyme
0.87
-
(S)-Lactate
-
-
0.94
-
(S)-Lactate
-
wild-type
3.6
-
(S)-Lactate
-
-
6.75
-
(S)-Lactate
-
A95G mutant
7.5
-
(S)-Lactate
-
R181K mutant
24.3
-
(S)-Lactate
-
25C, mutant enzyme E160G/V198I
25.5
-
(S)-Lactate
-
25C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
47.6
-
(S)-Lactate
-
35C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
50.7
-
(S)-Lactate
-
35C, mutant enzyme E160G/V198I
103
-
(S)-Lactate
-
R181M mutant
0.033
-
2,6-dichlorophenolindophenol
-
-
0.045
-
2-Hydroxyoctanoate
-
isoenzyme HAOX3
0.75
-
2-mercaptoethanol-glyoxylate adduct
-
-
-
0.04
-
2-oxo-octanoate
-
-
4.4
-
Bromopyruvate
-
transhydrogenation reaction
2.2
-
coenzyme A-glyoxylate adduct
-
-
0.28
-
dichlorophenolindophenol
-
cosubstrate: glycolate
4
-
DL-2-hydroxy-3-butynoate
-
-
0.38
-
DL-2-hydroxy-3-heptynoate
-
-
7
-
DL-2-hydroxy-3-hexynoate
-
-
0.14
-
DL-2-hydroxy-3-octynoate
-
-
9
-
DL-2-hydroxy-3-pentynoate
-
-
0.7
-
DL-2-hydroxy-4-methylthiobutanoic acid
-
-
1.1
-
DL-2-hydroxy-4-methylthiobutanoic acid
-
isozyme beta2
0.6
-
DL-2-Hydroxybutyrate
-
pH 7.0
0.6
-
DL-2-Hydroxybutyrate
-
-
1
-
DL-2-Hydroxybutyrate
-
pH 7.5
1.2
-
DL-2-Hydroxybutyrate
-
-
2.4
2.8
DL-2-Hydroxybutyrate
-
-
12.7
-
DL-2-Hydroxybutyrate
-
-
14
-
DL-2-Hydroxybutyrate
-
-
0.15
-
DL-2-hydroxycaproate
-
pH 7.5
0.25
-
DL-2-hydroxycaproate
-
pH 7.0
0.8
0.9
DL-2-hydroxycaproate
-
-
1.34
-
DL-2-hydroxycaproate
-
-
3.2
-
DL-2-hydroxycaproate
-
-
0.6
-
DL-2-hydroxyisocaproate
-
-
0.6
-
DL-2-hydroxyisovalerate
-
-
8
-
DL-2-hydroxyisovalerate
-
-
0.25
-
DL-2-hydroxyvalerate
-
pH 7.5
0.35
-
DL-2-hydroxyvalerate
-
pH 7.0
0.6
-
DL-2-hydroxyvalerate
-
-
13
-
DL-2-hydroxyvalerate
-
-
0.7
-
DL-3-chlorolactate
-
pH 7.5
0.8
-
DL-3-chlorolactate
-
pH 7.0
28
-
DL-3-chlorolactate
-
-
18
-
DL-alpha-hydroxy-n-butyrate
-
-
27
-
DL-alpha-hydroxy-n-butyrate
-
A95G mutant
5.5
-
DL-alpha-hydroxy-n-valerate
-
-
10
-
DL-alpha-hydroxy-n-valerate
-
A95G mutant
71
-
DL-alpha-phenyllactate
-
-
5
-
DL-glycerate
-
-
53
-
DL-glycerate
-
A95G mutant
2.04
-
DL-hydroxybutyrate
-
isozyme beta2
-
2.5
-
DL-hydroxybutyrate
-
isozyme beta1
-
27
-
DL-lactate
-
-
4
-
DL-methionine
-
pH 7.5
0.1
-
DL-phenyllactate
-
pH 7.0 and 7.5
10
-
DL-vinylglycolate
-
-
7.14
-
glycerate
-
pH 8.0
0.0056
-
glycolate
-
-
0.02
-
glycolate
-
pH 7.5, mesophyll cell isozyme
0.02
-
glycolate
-
mesophyll cell enzyme
0.056
-
glycolate
-
bundle sheath cell enzyme
0.058
-
glycolate
-
pH 7.5, bundle sheath cell isozyme
0.06
-
glycolate
-
leaf enzyme
0.1
-
glycolate
-
-
0.12
-
glycolate
-
isoenzyme HAOX1
0.141
-
glycolate
-
-
0.2
-
glycolate
-
pH 7.5, 30C, recombinant enzyme, first order
0.22
-
glycolate
-
cosubstrates: 2,4-dinitrophenyl hydrazone
0.23
-
glycolate
-
pH 7.0, 30C, recombinant enzyme, first order
0.24
-
glycolate
-
cosubstrate: O2
0.3
-
glycolate
-
-
0.31
-
glycolate
-
short chain oxidase
0.32
-
glycolate
-
-
0.42
-
glycolate
-
cosubstrate: 2,6-dichlorophenolindophenol
0.5
-
glycolate
-
-
2
-
glycolate
-
pH 9.0, 30C, recombinant enzyme, first order
2.1
-
glycolate
-
-
1.41
-
glyoxylate
-
cosubstrate: O2
1.78
-
glyoxylate
-
cosubstrate: 2,4-dinitrophenyl hydrazone
2.2
-
glyoxylate
-
-
3.4
-
glyoxylate
-
-
0.046
-
L-2-hydroxy octanoate
Q07523
-
1.36
-
L-2-hydroxy palmitate
Q07523
-
1.82
-
L-2-hydroxy-4-methylthiobutanoic acid
-
-
2.4
-
L-2-hydroxy-beta-methylvalerate
-
long chain oxidase
0.3
-
L-2-Hydroxyisocaproate
-
isozyme beta1
0.32
-
L-2-Hydroxyisocaproate
-
isozyme beta2
0.68
-
L-2-Hydroxyisocaproate
-
short chain oxidase
0.7
-
L-2-Hydroxyisocaproate
-
pH 7.5
0.9
-
L-2-Hydroxyisocaproate
-
pH 7.0
1.24
-
L-2-Hydroxyisocaproate
-
cosubstrate: 2,4-dinitrophenyl hydrazone
1.26
-
L-2-Hydroxyisocaproate
-
cosubstrate: O2
1.65
-
L-2-Hydroxyisocaproate
-
-
2.5
-
L-2-Hydroxyisocaproate
-
long chain oxidase
140
-
L-alpha-hydroxy-beta-methylvalerate
-
A95G mutant
125
-
L-alpha-hydroxy-isovalerate
-
A95G mutant
1.9
-
L-alpha-hydroxyphenyllactate
-
-
-
2.2
-
L-beta-Phenyllactate
-
long chain oxidase
0.34
-
L-lactate
-
4C, pH 7
0.94
-
L-lactate
-
25C, pH 7
1.8
-
L-lactate
-
pH 7.0
3.4
-
L-lactate
-
pH 7.5
4.68
-
L-lactate
-
-
4.7
-
L-lactate
-
isozyme beta2
5.6
5.7
L-lactate
-
-
6.1
-
L-lactate
-
isozyme beta1
8.5
-
L-lactate
-
-
9.3
-
L-lactate
-
-
16
-
L-lactate
-
short chain oxidase
16.5
-
L-lactate
-
-
5.3
-
L-leucine
-
isozyme beta2
6
-
L-leucine
-
pH 7.5
6.4
-
L-leucine
-
isozyme beta1
15
-
L-leucine
-
-
90
-
L-lysine
-
-
0.16
-
L-Mandelate
-
isozyme beta1
0.23
-
L-Mandelate
-
isozyme beta2
0.3
-
L-Mandelate
-
-
0.4
-
L-Mandelate
-
pH 7.5
0.8
-
L-Mandelate
-
pH 7.0
1.5
-
L-Mandelate
-
-
20
-
L-Mandelate
-
A95G mutant
53
-
L-methionine
-
-
0.09
-
L-Phenyllactate
-
isozyme beta1
0.13
-
L-Phenyllactate
-
isozyme beta2
35
-
L-tryptophan
-
pH 7.5
0.4
-
N-acetylcysteamine-glyoxylate adduct
-
-
0.022
-
O2
-
4C, pH 7
0.029
-
O2
-
R181K mutant
0.03
-
O2
-
R181M mutant
0.16
-
O2
-
wild-type
0.16
-
O2
-
25C, pH 7
0.3
-
O2
-
oxidation of 2-hydroxybutyrate
0.44
-
O2
-
pH 7.5, 30C, recombinant enzyme, first order
0.46
-
O2
-
oxidation of propane-1,3-dithiol-glyoxylate adduct
0.59
-
O2
-
pH 9.0, 30C, recombinant enzyme, first order
0.64
-
O2
-
pH 7.0, 30C, recombinant enzyme, first order
0.7
-
pantetheine-glyoxylate adduct
-
-
0.03
-
propane-1,3-dithiol-glyoxylate adduct
-
-
-
40
-
L-tryptophan
-
-
additional information
-
additional information
-
reduction rate constants and dissociation constants for reaction of lactate oxidases with alpha-1H- and alpha-2H-para-substituted mandelates
-
additional information
-
additional information
-
mesophyll isoform shows higher affinity for glycolate than bundle sheath isoform
-
additional information
-
additional information
Q07523
steady-state kinetics
-
additional information
-
additional information
-
stopped-flow, steady-state, and presteady-state kinetics at different pH values, pH profiles, detailed overview
-
additional information
-
additional information
-
Michaelis-Menten kinetics
-
additional information
-
additional information
Pediococcus sp.
-
Michaelis-Mentin kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
2-oxo-octanoate
-
-
0.36
-
Bromopyruvate
-
transhydrogenation reaction
1.9
-
DL-2-hydroxy-4-methylthiobutanoic acid
-
isozyme beta2
2.1
-
DL-2-hydroxy-4-methylthiobutanoic acid
-
isozyme beta1
0.76
-
DL-2-Hydroxybutyrate
-
-
1.66
-
DL-hydroxybutyrate
-
isozyme beta1
-
2
-
DL-hydroxybutyrate
-
isozyme beta2
-
54.1
-
flavin
-
pH 7.0, 30C, flavin reduction
1.04
-
glycerate
-
pH 8.0
0.33
-
glycolate
-
pH 7.0
3.6
-
glycolate
-
-
4.1
-
glycolate
-
-
15.6
-
glycolate
-
-
15.7
-
glycolate
-
pH 7.0, 30C, recombinant enzyme, first order
20
-
glycolate
-
pH 7.5, 30C, recombinant enzyme, first order
31.2
-
glycolate
-
pH 9.0, 30C, recombinant enzyme, first order
0.7
-
glyoxylate
-
-
0.83
-
glyoxylate
-
-
0.99
-
L-2-hydroxy octanoate
Q07523
-
0.34
-
L-2-hydroxy palmitate
Q07523
-
0.74
-
L-2-hydroxy-4-methylthiobutanoic acid
-
-
2
-
L-2-Hydroxyisocaproate
-
isozyme beta1
2.4
-
L-2-Hydroxyisocaproate
-
isozyme beta2
0.26
-
L-lactate
-
isozyme beta1
0.38
-
L-lactate
-
isozyme beta2
0.433
-
L-lactate
-
-
0.46
-
L-lactate
-
-
0.52
-
L-lactate
-
4C, pH 7
4.7
-
L-lactate
-
25C, pH 7
0.014
-
L-leucine
-
isozymes beta1 and beta2
0.11
-
L-Mandelate
-
-
1.55
-
L-Mandelate
-
isozyme beta1
2.51
-
L-Mandelate
-
isozyme beta2
0.59
-
L-Phenyllactate
-
isozyme beta1
0.52
-
O2
-
4C, pH 7
4.7
-
O2
-
25C, pH 7
0.7
-
L-Phenyllactate
-
isozyme beta2
additional information
-
additional information
-
reduction rate constants and dissociation constants for reaction of lactate oxidases with alpha-1H- and alpha-2H-para-substituted mandelates
-
additional information
-
additional information
-
a second-order rate constant for the capture of glycolate (kcat/Kglycolate) of 68300 M/s, and a second-order rate constant for reaction of the reduced flavin with oxygen (kcat/Koxygen) of 24500 Ms
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1400
-
O2
-
4C, pH 7
14738
1800
-
O2
-
25C, pH 7
14738
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.04
-
(R)-lactate
-
at pH 7.0
0.078
-
2,6-dichlorophenolindophenol
-
-
0.317
-
2-hydroxy butyrate
-
at pH 7.0
37
-
acetate
-
non-competitive, glycolate oxidation
48
-
acetate
-
non-competitive, glyoxylate reduction
494
-
acetate
-
decreasing values as the number of carbons in the alkyl side chain increases from 1 to 2 and to 5
3.6
-
Butyrate
-
non-competitive, glycolate oxidation
3
-
Caproate
-
-
280
-
chloride
-
pH 7.0, 25C
0.00169
-
Cibacron blue 3GA
-
at pH 6.0
0.27
0.39
diethyldithiocarbamate
-
competitive inhibition
0.77
-
diethyldithiocarbamate
-
competitive
0.13
-
dihydrolipoate
-
-
0.317
-
glycolate
-
at pH 7.0
36
-
glycolate
-
-
46
-
glycolate
-
-
12
-
glyoxylate
-
-
0.092
-
Heptanoate
-
non-competitive, glycolate oxidation
0.3
-
Hexanoate
-
non-competitive, glycolate oxidation
0.52
0.65
KCN
-
mixed-type inhibition
0.88
-
KCN
-
uncompetitive
23
-
L-leucine
-
-
0.3
-
L-Mandelate
-
at pH 7.0
92
-
L-Mandelate
-
-
8.2
-
malonate
-
non-competitive, glyoxylate reduction
0.03
-
NAD+
-
pH 7.4, 25C
0.44
-
oxalate
-
competitive, glycolate oxidation, non-competitive for glyoxylate oxidation
0.5
-
oxalate
-
at pH 7.0
0.75
-
oxalate
-
pH 8.0, versus glycerate
5
-
oxalate
-
-
10.5
-
oxalate
-
isozyme beta1
23
-
oxalate
-
isozyme beta2
171
-
Oxamate
-
-
2.5
-
Phenyllactate
-
competitive
9.5
-
Propionate
-
non-competitive, glycolate oxidation
17
-
Propionate
-
non-competitive, glyoxylate reduction
126
-
Propionate
-
-
15.9
-
pyruvate
-
isozyme beta1
18.3
-
pyruvate
-
isozyme beta2
14
-
succinate
-
competitive, glycolate oxidation
1
-
trans-Cinnamate
-
isozyme beta1
1.9
-
trans-Cinnamate
-
isozyme beta2
1.2
-
valerate
-
non-competitive, glyoxylate reduction
1.3
-
valerate
-
non-competitive, glycolate oxidation
9.2
-
malonate
-
competitive, glycolate oxidation
additional information
-
additional information
-
straight-chain monocarboxylic acids are non-competitive inhibitors with either glycolate or glyoxylate as substrates, dicarboxylic acids are competitive inhibitors with glycolate as substrate, but non-competitive inhibitors for glyoxylate as substrate
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0007
-
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0108
-
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0012
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0054
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0095
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0107
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00427
-
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
427
-
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0006
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0124
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0005
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0104
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0002
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0226
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0011
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00812
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0017
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0022
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0007
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0023
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0013
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0134
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0004
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0315
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0135
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00523
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0013
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0073
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00912
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0357
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00634
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.002
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0113
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0004
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0083
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0011
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0051
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0267
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.048
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0083
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0009
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0088
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.003
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0076
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0005
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0062
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0002
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00113
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00095
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0358
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0137
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0196
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0008
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
11
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0032
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0407
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0006
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0339
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0007
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00714
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00135
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0031
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0091
-
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0009
-
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0052
-
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0005
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0205
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0002
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0186
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0011
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0032
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0135
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0116
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0217
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0003
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0166
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0004
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.01125
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0009
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0095
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0009
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0054
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0052
-
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0318
-
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.00091
-
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0004
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0022
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0008
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0042
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0005
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0021
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0011
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0018
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
pH and temperature not specified in the publication
3.7
-
Mandelate
-
-
1.8
-
oxalate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.28
-
-
-
0.45
-
-
-
0.45
-
-
pH 7.5, 25C, mesophyll isoform
0.55
-
-
pH 7.5, 25C, bundle sheath isoform
0.55
-
-
purified mesophyll cell isozyme
0.62
-
-
purified whole leaf enzyme
0.65
-
-
purified native enzyme from leaves
0.78
-
-
isozyme beta1
0.88
-
-
isoenzyme B
1.2
-
-
-
1.33
-
-
purified bundle sheath cell isozyme
2.08
-
-
-
2.4
4.8
-
liver enzyme
3.66
-
-
isoemzyme A
20
-
Pediococcus sp.
-
commercial preparation, pH not specified in the publication, temperature not specified in the publication
25.43
-
-
-
28.07
-
A9QH69, A9QH71
type 1 enzyme expressed in Escherichia coli BL21Star, 10 mM potassium phophate, pH 6,5, 0.01 mM flavin adenine nucleotide, 37C, 0.02% 2,2-azinobis (3-ethylbenzthiazolinesulfonic acid), 10 mM L-(+)-lactate, 0.5 U horseradish peroxidase (peroxidase-coupled spectrophotometric assay)
41
-
Pediococcus sp.
-
commercial preparation, pH 7.0, temperature not specified in the publication
45.76
-
A9QH69, A9QH71
type 2 enzyme expressed in Escherichia coli BL21Star, 10 mM potassium phophate, pH 6.5, 0.01 mM flavin adenine nucleotide, 37C, 0.02% 2,2-azinobis (3-ethylbenzthiazolinesulfonic acid), 10 mM L-(+)-lactate, 0.5 U horseradish peroxidase (peroxidase-coupled spectrophotometric assay)
72
-
Pediococcus sp.
-
commercial preparation, pH not specified in the publication, temperature not specified in the publication
1546
-
-
purified native enzyme from mesophyll bundle sheath
additional information
-
-
decrease of enzyme activity upon oxidative stress induced by glutathione depletion or postischemic perfusion
additional information
-
-
metabolism of glycolate by maize leaf discs in darkness in a segregating mutant population with varying GO activities, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
-
Pediococcus sp.
-
phosphate buffer, optimal operating conditions
7
-
-
assay at
7
-
-
assay at
7
-
Pediococcus sp.
-
assay at
7.3
-
-
bundle sheath isoform
7.4
-
-
assay at
7.5
-
-
mesophyll isoform
7.5
-
-
assay at
7.5
-
-
-
7.7
-
-
short chain oxidase
7.9
-
-
long chain oxidase
8
-
-
oxidation of L-lactate
8.4
-
-
-
8.6
8.9
-
substrate: DL-2-hydroxybutyrate
8.7
-
-
oxidation of L-leucine
8.8
-
-
-
8.8
-
Pediococcus sp.
-
0.1 M Tris buffer, compromise between optimal lactate oxidase pH 7.5 and optimal pH of 9.5 for peroxidase from Arthromyces ramosus in the combined biosensor system
8.9
9.4
-
substrate: DL-2-hydroxyisocaproate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-
pH profiles, the enzyme shows a ping-pong bi-bi kinetic mechanism between pH 6.0 and 10.0, overview
6
9
-
L-LAC-OX activity is rather constant in 6.0-9.0 pH range
8.3
9.5
-
80% of the maximum activity within
additional information
-
-
the dependence of GO activity on pH is bell-shaped
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
25
-
Pediococcus sp.
-
assay at
30
-
-
assay at
37
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
Q9CG58
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
main location of the enzyme activity
Manually annotated by BRENDA team
-
distribution of isoenzyme HAOX2
Manually annotated by BRENDA team
-
isoenzyme L-2-hydroxyacid oxidase B
Manually annotated by BRENDA team
-
two forms: long chain oxidase, short chain oxidase
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
-
mesophyll and bundle sheath
Manually annotated by BRENDA team
-
of seedling
Manually annotated by BRENDA team
-
from 18-days-old seedlings
Manually annotated by BRENDA team
-
distribution of isoenzymes HAOX1, HAOX2
Manually annotated by BRENDA team
-
isoenzyme L-2-hydroxyacid oxidase A
Manually annotated by BRENDA team
-
isoenzyme L-2-hydroxyacid oxidase A
Manually annotated by BRENDA team
-
distribution of isoenzymes HAOX1, HAOX3
Manually annotated by BRENDA team
additional information
-
hepatic or leaf glycolate oxidases oxidize best glycolate and alpha-hydroxyisocaproate, that from kidney oxidizes only long-chain alpha-hydroxy acids; Kidney enzyme oxidizes only long-chain alpha-hydroxy acids. The liver enzyme also oxidizes L-amino acids
Manually annotated by BRENDA team
additional information
plant, Rattus sp.
-
hepatic or leaf glycolate oxidases oxidize best glycolate and alpha-hydroxyisocaproate, that from kidney oxidizes only long-chain alpha-hydroxy acids
Manually annotated by BRENDA team
additional information
-
influence of growth conditions on enzyme expression, overview
Manually annotated by BRENDA team
additional information
-
one isoform is located in bundle sheath cells, the second isozyme has dual location, and the third one is located in mesophyll cells
Manually annotated by BRENDA team
additional information
-
the enzyme is expressed throughout the growth phase, and expression of the lox gene increases by about 2.5fold when cells enter the stationary phase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
preparation of heavy and light mitochondria, 2 distinct molecular forms
Manually annotated by BRENDA team
-
; confocal immunofluorescence microscopy reveals that capsid protein P8 is colocalized with GOX in peroxisomes
Manually annotated by BRENDA team
Q19U05
the enzyme contains a peroxisomal targeting signale -ARL
Manually annotated by BRENDA team
additional information
-
subcellular localization analysis, no enzyme activity in cytosol, mitochondrial membrane, or mitochondrial matrix, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40950
-
Q9CG58
MALDI-TOF MS, calculated, 383 amino acids
41290
-
-
determined by mass spectrometry. After tag-removal two close bands appear on SDS-PAGE one at 45.287 kDa and one at 41.288 kDa
42380
-
A9QH69, A9QH71
calculated, 390 amino acids, 869 bp
44040
-
A9QH69, A9QH71
calculated, 407 amino acids, 920 bp, 51 bp repeat sequence compared to type 1 enzyme
45290
-
-
determined by mass spectrometry. After tag-removal two close bands appear on SDS-PAGE one at 45.287 kDa and one at 41.288 kDa
80000
-
-
gel filtration
88900
-
-
sedimentation equilibrium analysis
150000
-
-
isoenzymes A and B, gel filtration, sedimentation equilibrium analysis, self-association at low protein concentrations
160000
-
-
sequence calculation
169000
-
-
non-denaturating gel electrophoresis
187300
-
-
gel filtration
190000
-
-
gel filtration
250000
-
-
sedimentation equilibrium analysis
300000
-
-
gel filtration
400000
-
-
native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, isoenzymes A and B, SDS-PAGE
?
-
x * 37000, isoenzymes A and B, SDS-PAGE
?
-
x * 51100, calculation from amino acid composition
?
-
x * 44000, bundle sheath cell isozyme, SDS-PAGE, x * 37000, mesophyll cell isozyme, SDS-PAGE
?
Q9CG58
x * 39000, calculated
?
-
x * 39000, about, sequence calculation
monomer
A9QH69, A9QH71
1 * 42384, type 1 enzyme; 1 * 44038, type 2 enzyme
octamer
-
8 * 50000, transmission electron microscopy analysis and SDS-PAGE
octamer
-
-
tetramer
-
4 * 37800, SDS-PAGE
tetramer
-
4 * 47500, SDS-PAGE
tetramer
-
4 * 48200, SDS-PAGE
tetramer
-
gel filtration
tetramer
-
2 x 37000 + 2 * 44000, SDS-PAGE
monomer
Streptococcus iniae QMA0177
-
1 * 44038, type 2 enzyme
-
additional information
Q07523
structure analysis, modelling, the enzyme shows the same beta8alpha8 TIM barrel structure as other structurally characterized family members of the FMN-dependent enzyme family
additional information
-
gene glcD encodes the D-subunit of the glycolate oxidase
additional information
-
quaternary structure of C3 plant GO, overview
additional information
-
molecular modeling studies using the rat Hao2 crystal structure, PDB ID 1TB3, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
enzyme-sulfite complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3.0 A resolution, octamer with non-crystallographic two- and four-fold axes
-
hanging-drop or sitting-drop vapour diffusion method, 2.44 A resolution, large diffracting crystals of LOXR181M are obtained. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632 A, c= 200.263 A, alpha = beta = gamma =90. There are four monomers in the asymmetric unit
-
resolution to 1.9 A. One pyruvate molecule is bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265
-
sitting-drop vapor diffusion technique. Crystal structure of wild-type enzyme at 2.1 A resolution. Space group I422 of unit-cell parameters a = b = 191.096 A, c = 194.497 A and alpha = beta = gamma = 90 with four monomers per asymmetric unit
-
sitting-drop vapour-diffusion method, determination of structure at 2.1 A resolution
-
unbound enzyme and in complex with D-lactate, both at pH 4.5. In the complex structure, the D-lactate resides in the substrate-binding site, but an active site base, His265, flips far away from the D-lactate, as compared with its conformation in the unbound state at pH 8.0. The flip of His265 triggers a large structural rearrangement, creating a new hydrogen bonding network between His265-Asp174-Lys221 and, furthermore, brings molecular oxygen in between D-lactate and His265. In the mechanism of the subsequent oxidative half-reaction, His265 flips back, pushing molecular oxygen into the substrate-binding site as the second substrate, and the reverse reaction takes place to produce hydrogen peroxide
-
structures of recombinant GO complexed with sulfate, glyoxylate, and 4-carboxy-5-dodecylsulfanyl-1,2,3-triazole (CDST), determined by X-ray crystallography are reported. A loop region (loop 4), is completely visible when the GO active site contains a small ligand. Lack of electron density for this loop in the GOCDST complex, mimicking a large substrate, indicates that a disordered to ordered transition occurs with substrate binding. Conformational flexibility of Trp110 is responsible for enabling GO to react with R-hydroxy acids. Movement of Trp110 disrupts a hydrogen-bonding network between Trp110, Leu191, Tyr134, and Tyr208. This loss indicates that active site movements are directly linked to changes in the conformation of loop 4
-
study of the nanomechanical properties of lactate oxidase monolayer immobilized on gold substrate by atomic force microscopy. The data fit by the Hertz model for a conical indenter, an average value of Young's modulus for the protein layer is in the 0.5-0.8 GPa range
Pediococcus sp.
-
sitting drop vapor diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein in 0.1 M Tris, pH 7.5, mixed with the same volume of reservoir solution containing 0.4 M sodium acetate and 0.2 M sodium citrate, pH 6.5, equilibration at 4C, soaking of crystals in 25% glycerol-containing reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution
Q07523
ammonium sulfate precipitation, 2.6 A resolution of a two subunit apoenzyme
-
tert-butanol precipitation, bound active-site inhibitors
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
half-maximum oxidation rate
8
11
-
stable for 15 min at 30C
9
-
-
half-maximum oxidation rate
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
-
t1/2: 1.7 min for wild-type enzyme, 30.3 min for mutant enzyme E160G/V198I, 61.4 min for mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
addition of 0.03 mM FMN increases the stability about 30% after 10 d of storage
-
addition of MnCl2, Dextran 500000, glycerol or octyl glucopyranoside increase stability after 10 d of incubation at 4C, HgCl2 and SDS destabilizes
-
human albumin protects against loss of acitivity during freezing and thawing
-
loss of activity due to loss of irreversibly removed FMN during storage
-
long chain oxidase stable at -20C, short chain oxidase stable at -20C for several months
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
isopropanol
Pediococcus sp.
-
lactate oxidase retains with more than 60% of it is initial activity after exposing to water-isopropanol mixtures with over 90% v/v content of organic solvent
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, lyophilized powder containing 70-80% sucrose, stable for more than a year
-
4C, 10 mM Tris-HCl, 15 mM NaCl, 0.02 mM FMN, 1 mM EDTA, several weeks, cannot be stored frozen at -20C or -80C
-
-70C, concentrated solution, stable for several months
-
below 0C, 0.1 mol/l phosphate buffer, pH 7.2 (potassium and sodium salts), 2.2 mg lactate oxidase in 0.5 ml buffer, enzymatic activity stable for several weeks
Pediococcus sp.
-
4C, 60% ammonium sulfate precipitate, several months
-
-5C, 3.2 M ammonium sulfate, pH 8.3, 0.002 M FMN
-
-20C, ammonium sulfate precipitate or in solution with 2.5 M glycerol, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification via dye affinity chromatography
-
tissue-specific isozymes from leaves 63.5fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography, bundle sheath cell isozyme and mesophyll cell isozyme to homogeneity
-
to homogeneity, chromatography techniques
-
native enzyme from leaves 207fold by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, and again gel filtration
-
purified in one step on hydroxyapatite column onto which it is strongly adsorbed. For the initial purification steps, FMN is added to the buffers
-
recombinant enzyme by nickel affinity chromatography, ammonium sulfate fractionation and dialysis
-
recombinant isoenzymes
-
using a Ni-NTA-column, gel filtration and ion-exchange chromatography
-
partial, isoenzymes A and B
-
native enzyme, subcellular fractionation
-
near homogeneity, precipitation techniques
-
recombinant isozymes beta1, beta2
-
to crystalline state, chromatography and precipitation techniques
-
to homogeneity, 2-step chromatography
-
to homogeneity, chromatography steps
-
native enzyme from leaves to homogeneity
-
recombinant enzyme
-
to crystalline state, precipitation techniques
-
to crystalline state, recombinant enzyme
-
to homogeneity
-
centrifugation, washing with 10 mM potassium phosphate buffer, pH 6.5, stored at -20C, resuspended with same buffer, treated with lysozyme followed by disruption with glass beads in a bead mill, centrifugation, supernatants used for enzyme assays; centrifugation, washing with 10 mM potassium phosphate buffer, pH 6.5, stored at -20C, resuspended with same buffer, treated with lysozyme followed by disruption with glass beads in a bead mill, centrifugation, supernatants used for enzyme assays
A9QH69, A9QH71
to crystalline state, chromatography and precipitation techniques
-
to homogeneity, chromatography techniques, 2 distinct forms
-
native enzyme from maize leaf bundle sheath 46.6fold by gel filtration, anion exchange chromatography, and again gel filtration. Native enzyme 10.5fold from leaf mesophyll, by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, and again gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli DH1
-
expression in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli, expression in human skin fibroblasts
-
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
-
co-expression of the enzyme with the Rice dwarf virus, RDV, outer capsid P8 protein in Spodoptera frugiperda cells, the localization of P8 in Spodoptera frugiperda cells changed from diffuse to discrete, punctuate inclusions during expression from 24 to 48 h post inoculation, coexpression of GOX with P8 may target P8 into peroxisomes, which serve as replication sites for a number of viruses
-
determination of at least five putative GLO gene members in the rice genome, which are located on chromosome 3, 4, and 7, respectively
-, Q10CE4
DNA and amino acid sequence determination and analysis, quantitative expression analysis, the gene contains a GOX-like-riboflavin-5'-phosphate conserved domain and a predicted adenosine-5'-(a-thio)diphospho-5'-ribofuranosylnicotinamide NAD binding domain
Q19U05
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
-
expression in Escherichia coli
-
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
Roseobacter sp.
-
coexpression of glycolate oxidase and catalase T in Pichia pastoris
-
expression in Escherichia coli
-
expression in Pichia pastoris
-
high-level expression in Escherichia coli
-
PCR-amplification, expression in Escherichia coli BL21 Star; PCR-amplification, expression in Escherichia coli BL21 Star
A9QH69, A9QH71
gene GO1, DNA and amin acid sequence determination and analysis, phylogenetic tree
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Arabidopsis thaliana plants overexpressing glycolate oxidase in chloroplasts accumulates both hydrogen peroxide and glyoxylate, enzyme-overexpressing plants show retarded development, yellowish rosettes, and impaired photosynthetic performance. The plants develop oxidative stress lesions under photorespiratory conditions but grow like wild-type plants under nonphotorespiratory conditions
Q56ZN0
the suppression effect of estradiol is dependent on the concentration of estradiol. A reduction of about 60% is observed when 0.001 mM estradiol is applied for 10 d, and the maximal reduction of over 90% occurs at 0.005 mM
-, Q10CE4
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A95G
-
enhanced activity with bulky substrates, increase in the reduction rate constants with substrates having a bulky alpha-substituent such as mandelate, when compared with wild-type enzyme
A95G
-
much enhanced oxidase activity with longer chain L-alpha-hydroxyacids such as alpha-hydroxy-n-butyric acid, alpha-hydroxy-n-valeric acid and L-mandelic acid
E160G/V198I
-
the half-life of the mutant lactate oxidase at 70C is about 18times that of the wild-type enzyme. Km-value for (S)-lactate at 25C is 46fold higher than wild-type value, Km-value for (S)-lactate at 25C is 59fold higher than wild-type value
E160G/V198I/G36S/T103S/A232S/F277Y
-
the half-life of the mutant lactate oxidase at 70C is about 2 times that of E160G/V198I mutant and about 36 times that of the wild-type enzyme. Km-value for (S)-lactate at 25C is 48fold higher than wild-type value, Km-value for (S)-lactate at 25C is 55fold higher than wild-type value. Mutant is obtained by direct evolution
R181K
-
less active than wild-type
R181K/R268K
-
no activity
R181M
-
less active than wild-type
H260A
-
site-directed mutagenesis
R268K
-
no activity
additional information
Q56ZN0
Arabidopsis thaliana plants overexpressing glycolate oxidase in chloroplasts accumulates both hydrogen peroxide and glyoxylate, enzyme-overexpressing plants show retarded development, yellowish rosettes, and impaired photosynthetic performance. The plants develop oxidative stress lesions under photorespiratory conditions but grow like wild-type plants under nonphotorespiratory conditions, phenotype, overview
H260Q
-
site-directed mutagenesis
additional information
-
co-expression of GOX with capsid protein P8 targets capsid protein P8 into peroxisomes: time course analysis demonstrates that the localization of capsid protein P8 in peroxisomes of Spodoptera frugiperda cells, co-expressing capsid protein P8 and GOX, changes from diffuse to discrete, punctuate inclusions during expression from 24 to 48 h post inoculation; yeast two-hybrid and co-immunoprecipitation assays indicate that capsid protein P8, an outer capsid protein of Rice dwarf phytoreovirus (RDV), interacts with rice glycolate oxidase (GOX)
additional information
-, Q10CE4
phenotypes of GLO-suppressed plants under air and high CO2, overview. The plants with 30%, 60%, and 90% reduced GLO activities accumulate 40, 60, and 130fold, respectively, more glycolate than the wild-type
additional information
Pediococcus sp.
-
immobilization of the enzyme from water-organic solvent mixture on biosensor membranes, most active enzyme containing membranes are obtained using triethoxysiloxanes: gamma-aminopropyl-,vinyl-, or phenyl-triethoxysiloxane, method optimization and evaluation, overview. Lactate oxidase remains with more than 60% of it is initial activity after exposing to water-isopropanol mixtures with over 90% v/v content of organic solvent
additional information
Pediococcus sp.
-
imobilization of the enzyme on gold electrodes, determination of lactate oxidase patterns with gold substrates, in terms of homogeneity, compactness and stability, overview. LOx is directly stamped to a bare gold surface, LOx is previously covalently bonded to a thiolated molecule, dithiodipropionic acid di-N-succinimidyl ester, and this conjugate is transferred from an elastomeric stamp to a bare gold substrate, formation of a LOx/DTSP micropattern on a bare gold surface, which is followed by exposure to a solution containing hexadecylmercaptane
additional information
Pediococcus sp.
-
construction and evaluation of a biosensor of chiral, biocompatible, conducting material comprising collagen I, silica gel and ferrocene involving glucose oxidase/lactate oxidase enzymes. Preparation of the ferrocene/collagen or ferrocene/collagen/silica modified electrodes. The material modifies and inverts the chiral selectivity of D-glucose oxidase and L-lactate oxidase in collagen incorporated in tetramethoxysilane, overview
additional information
-
in an enzyme disruption mutant, the highest concentration of H2O2 attained in the medium is found to be approximately 1 mM, about one-fifth the level for the parental strain. Although cell growth continuous until glucose in the medium becomes undetectable even in the absence of added catalase, the maximum cell mass attained is considerably higher in the presence of catalase than in its absence. The maximum cell mass achieved in the presence of added catalase is reproducibly lower by 0.2 to 0.3 turbidity units than that of the parent
additional information
Streptococcus pneumoniae GTC13809
-
in an enzyme disruption mutant, the highest concentration of H2O2 attained in the medium is found to be approximately 1 mM, about one-fifth the level for the parental strain. Although cell growth continuous until glucose in the medium becomes undetectable even in the absence of added catalase, the maximum cell mass attained is considerably higher in the presence of catalase than in its absence. The maximum cell mass achieved in the presence of added catalase is reproducibly lower by 0.2 to 0.3 turbidity units than that of the parent
-
additional information
-
the GO knockout mutation mutant, with themutant allele go1-m1::Ac, leads to a segregated seedling lethal phenotype
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
enzyme is used in clinical chemistry for the determination of (S)-lactate in blood in some pathological diseases such as diabetes, heart diseases and shock syndrome
synthesis
-
optimization of production of lactate oxidase by cultivating strains under high aeration in a medium with 0.5% glucose and 2% lactate for 1 day results in activities of 130-140 U/l
drug development
-
in humans the enzyme is a potential drug target for treatment of primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
molecular biology
-
the interaction of capsid protein P8 with the GOX of host cells leads to translocation of capsid protein P8 into peroxisomes. The interaction between capsid protein P8 and GOX plays important roles in Rice dwarf phytoreovirus targeting into the replication site of host cells
analysis
Pediococcus sp.
-
development of a lactate biosensor through immobilization of lactate oxidase in an albumin and mucin composed hydrogel by gluitaraldehyde cross-linking and trapping between two polycarbonate membranes. Hydrogen peroxide produced is detected on a platinum electrode. The response time of the sensor to 0.010 mM lactate requires 90 s to give a 100% steady-state response of 0.079 microA. Linear behavior is obtained between0.7 microM and 1.5 mM. The detection limit calculated from the signal to noise ratio was 0.7 microM
diagnostics
Pediococcus sp.
-
lactate biosensor development based on an enzymatic recognition system using lactate oxidase and a transduction system based on laminol, peroxidase from Arthromyces ramosus and metallic aluminum, immobilized in a plastic support by a polyion complex membrane prepared from poly-L-lysine hydrobromide and poly(sodium 4-styrenesulfonate)
diagnostics
Pediococcus sp.
-
lactate biosensor (FIA amperometric detection), tested with beer samples, detection limit: 0.84 micromol/l, three-electrode cell with AG/AGCl, NaCl reference electrode, platinum wire, glassy carbon electrode, the latter layered with Prussian Blue film of K3Fe(CN)6, Fe(III), KCl, cetyltrimethylammonium bromide, pH 1.7 maintained with HCl, lactate oxidase immobilized onto the Prussian Blue-modified glassy carbon electrode, enzyme layer covered by a Nafion-ethanol solution, storage in phosphate buffer, pH 6.9
drug development
-
isozyme Hao2 is a target for drug development in high blood pressure
medicine
-
decrease of enzyme activity upon oxidative stress induced by glutathione depletion or postischemic perfusion, down-regulation of enzyme as mechanism to prevent excessive H2O2 formation in liver peroxisome
synthesis
-
production of glyoxylate in biocatalysis of co-produced glycolate oxidase and catalase T
synthesis
-
-
synthesis
-
optimization of enzyme expression in Escherichia coli for production glyoxylate in culture medium