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Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase
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1.1.3.15 (S)-2-hydroxy-acid oxidaseIUBMB Comments
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.
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Word Map
- 1.1.3.15
- venom
- snake
- catalase
-
biosensors
- laaos
-
electrode
- glyoxylate
- oxidases
-
electrochemical
-
amperometric
-
photorespiration
- oxalate
-
photorespiratory
- bothrops
-
d-amino
- crotalus
- hyperoxalurias
- viper
- antivenoms
- hydroxypyruvate
- microbodies
-
snakebite
-
crisp
- calloselasma
- cobra
- rhodostoma
- trimeresurus
-
thrombin-like
-
glyoxysomes
- agkistrodon
- kaouthia
- rattlesnake
- viridans
- adamanteus
-
screen-printed
-
flavocytochrome
-
malayan
-
elapid
-
fmn-dependent
- phosphomonoesterase
-
svmps
-
viperids
- hannah
- l-leu
- aerococcus
- daboia
- atrox
- drug development
- diagnostics
- medicine
- synthesis
-
bradykinin-potentiating
- analysis
- molecular biology
-
three-finger
- agriculture
-
nafion
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
(L)-2-HAOX, (S)-2-hydroxy-acid oxidase, peroxisomal, 2-hydroxy acid oxidase, CSUB_C1080, GLO, Glo1, GLO3, Glo4, glycolate oxidase, GO, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-2-hydroxy-acid oxidase, peroxisomal
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-
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glycolate oxidase
GO
GOX
HAO1
Hao2
HAOX1
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-
-
-
HAOX2
-
-
-
-
HAOX3
-
-
-
-
hydroxy-acid oxidase A
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hydroxy-acid oxidase B
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hydroxyacid oxidase 1
hydroxyacid oxidase A
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L-2-hydroxy acid oxidase
L-alpha-hydroxy acid oxidase
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L-lactate oxidase
lactate oxidase
LctO
long chain L-2-hydroxy acid oxidase 2
long-chain 2-hydroxy acid oxidase
LOX
oxidase, L-2-hydroxy acid
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-
-
-
additional information
the enzyme belongs to the FMN-dependent enzyme family
glycolate oxidase
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GOX
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-
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L-2-hydroxy acid oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
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
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-
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an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
the catalytic residue is Phe23, reaction mechanism
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
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
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
reaction mechanism, quantum mechanics/molecular mechanics calculations and molecular dynamics simulations, overview. LCHAO-catalyzed dehydrogenation of L-lactate is a stepwise catalytic reaction in a hydride transfer mechanism but not a carbanion mechanism. In contrast to the wild-type enzyme, the mutant Y129F LCHAO catalyzes the oxidation of L-lactate in one step
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9037-63-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxybutanoate + + 2,6-dichlorophenolindophenol
2-oxobutanoate + reduced 2,6-dichlorophenolindophenol
preferred substrate
-
-
?
(R)-lactate + + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
preferred substrate
-
-
?
2-hydroxybutanoate + bromopyruvate + ?
bromolactate + pyruvate + ?
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transhydrogenation reaction
-
?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
-
-
-
?
2-hydroxydodecanoate + O2
2-oxododecanoate + H2O2
-
-
-
?
2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxo-octanoate + reduced 2,6-dichlorophenolindophenol
-
-
-
r
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
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?
DL-2-hydroxy-3-butynoate + O2
2-oxo-3-butynoate + H2O2
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good substrate, but inactivation after 25 turnovers
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?
DL-2-hydroxy-3-heptynoate + O2
2-oxo-3-heptynoate + H2O2
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86% of the activity compared to DL-2-hydroxybutyrate
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?
DL-2-hydroxy-3-hexynoate + O2
2-oxo-3-hexynoate + H2O2
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65% of the activity compared to DL-2-hydroxybutyrate
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?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
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70% of the activity compared to DL-2-hydroxybutyrate
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?
DL-2-hydroxy-3-pentynoate + O2
2-oxo-3-pentynoate + H2O2
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2fold higher activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-4-methylmercaptobutyrate + 2,6-dichlorophenolindophenol
2-oxo-4-methylmercaptobutyrate + reduced 2,6-dichlorophenolindophenol
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good substrate for long chain oxidase, low activity for short chain oxidase
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?
DL-2-hydroxy-4-methylthiobutanoic acid + 2,6-dichlorophenolindophenol
2-oxo-4-methylthiobutanoic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-2-hydroxybutyrate + 2,4-dinitrophenylhydrazine
2-oxobutyrate 2,4-dinitrophenylhydrazone
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low activity
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?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol
2-oxocaproate + reduced 2,6-dichlorophenolindophenol
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low activity for short chain oxidase, moderate activity for long chain oxidase
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?
DL-2-hydroxydecanoate + 2,6-dichlorophenolindophenol
2-oxodecanoate + reduced 2,6-dichlorophenolindophenol
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good substrate for long chain oxidase, traces of activity for short chain oxidase
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?
DL-2-hydroxyisovalerate + 2,4-dinitrophenylhydrazine
2-oxoisovalerate 2,4-dinitrophenylhydrazone
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very low activity
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?
DL-2-hydroxyisovalerate + 2,6-dichlorophenolindophenol
2-oxoisovalerate + reduced 2,6-dichlorophenolindophenol
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no activity for short chain oxidase, moderate activity for long chain oxidase
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?
DL-2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxooctanoate + reduced 2,6-dichlorophenolindophenol
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good substrate for long chain oxidase, no activity for short chain oxidase
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?
DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol
2-oxovalerate + reduced 2,6-dichlorophenolindophenol
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low activity for short chain oxidase, moderate activity for long chain oxidase
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?
DL-3-indolelactate + 2,6-dichlorophenolindophenol
3-indolepyruvate + reduced 2,6-dichlorophenolindophenol
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good substrate for long chain oxidase, no activity for short chain oxidase
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?
DL-3-methoxy-4-hydroxymandelate + 2,6-dichlorophenolindophenol
(3-methoxy-4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
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-
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?
DL-beta-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
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no activity for short chain oxidase
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?
DL-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
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low activity
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?
DL-mandelate + O2
phenylglyoxylic acid + H2O2
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol
(4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
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no activity for short chain oxidase
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?
DL-p-hydroxymandelate + O2
?
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
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90% of the activity compared to DL-2-hydroxybutyrate
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?
glycolate + 2,4-dinitrophenylhydrazine
glyoxylate 2,4-dinitrophenylhydrazone
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best substrate tested
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?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
glycolate + phenazine methosulfate
glyoxylate + reduced phenazine methosulfate
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?
glyoxylate + 2,4-dinitrophenylhydrazine
oxalate 2,4-dinitrophenylhydrazone
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25% of the activity compared to glycolate
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?
glyoxylate thiohemiacetals + O2
? + H2O2
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possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
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?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
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oxidative decarboxylation
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?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
L-2-hydroxyisocaproate + 2,4-dinitrophenylhydrazine
2-oxoisocaproate 2,4-dinitrophenylhydrazone
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-
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?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
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-
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?
L-2-hydroxyisocaproate + O2
4-methyl-2-oxopentanoate + H2O2
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100% activity with long chain oxidase, 32% activity with short chain oxidase
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r
L-4-chloromandelate + O2
?
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
L-4-fluoromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
L-4-methoxymandelate + O2
?
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
L-4-methylmandelate + O2
?
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
L-4-nitromandelate + O2
?
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
L-4-trifluoromethylmandelate + O2
?
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the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
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?
L-lactate + 2,4-dinitrophenylhydrazine
pyruvate 2,4-dinitrophenylhydrazone
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very low activity
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?
L-lactate + phenazine methosulfate
? + reduced phenazine methosulfate
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-
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?
L-leucine + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
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-
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?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
mandelate + O2
phenylpyruvate + H2O2
oxidation of an L-2-hydroxy acid to a 2-oxoacid, model for the binding of L-mandelate into the active site, overview
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?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
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may be the physiological substrates
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?
(S)-lactate + O2
acetate + CO2 + H2O
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glucose-repressible lactate oxidase is likely responsible for H2O2 production
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-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
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?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
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substrates for isoenzymes HAOX1, HAOX2
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?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
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?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
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-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
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-
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?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
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-
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?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
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48% of the activity compared to glycolate
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?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
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?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
low activity for long chain oxidase, no activity for short chain oxidase
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?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
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68% of the activity compared to glycolate
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?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
higher affinity with C5 and C6 hydroxy acids
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?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
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low activity
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?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
39% of the activity compared to glycolate
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?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
low activity
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?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
best substrate tested
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
highest activity for short chain oxidase, no activity for long chain oxidase
-
?
glycolate + O2
glyoxylate + H2O2
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highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
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the catalytic adduct is formed by hydrogen abstraction from the re-face of glycolate
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-
?
glycolate + O2
glyoxylate + H2O2
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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
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preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glyoxylate + O2
? + H2O2
-
26% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
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in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
lower activity for preparation from "heavy" mitochondria
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-lactate + O2
pyruvate + H2O2
-
high activity, does not act on D-lactate
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-mandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
lactate + O2
pyruvate + H2O2
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
no substrates: D-alanine, pyruvate, D-glucose, L-alanine, ethanol and L-lactate
-
-
-
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
?
-
-
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
?
-
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
?
-
-
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
?
-
the enzyme is involved in the photorespiration process
-
-
?
additional information
?
-
the enzyme is not able to metabolize D-lactate
-
-
?
additional information
?
-
-
the enzyme is not able to metabolize D-lactate
-
-
?
additional information
?
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
?
additional information
?
-
-
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
?
-
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
-
-
-
?
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
glyoxylate thiohemiacetals + O2
? + H2O2
-
possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
-
oxidative decarboxylation
-
?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
may be the physiological substrates
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
48% of the activity compared to glycolate
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
68% of the activity compared to glycolate
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
higher affinity with C5 and C6 hydroxy acids
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
low activity
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
39% of the activity compared to glycolate
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
low activity
-
?
glycolate + O2
glyoxylate + H2O2
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
-
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
-
preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
?
glyoxylate + O2
? + H2O2
-
26% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-lactate + O2
pyruvate + H2O2
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-lactate + O2
pyruvate + H2O2
-
high activity, does not act on D-lactate
-
?
lactate + O2
pyruvate + H2O2
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
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
?
-
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
?
-
-
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
?
-
the enzyme is involved in the photorespiration process
-
-
?
additional information
?
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
?
additional information
?
-
-
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
?
-
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
three-residue insertion of loop 4 in isozyme beta2 influences ionisation state of FMN
FMN
-
both FMN and FAD, with FAD 46.8% of the activity with FMN
FMN
the enzyme contains a GOX-like-riboflavin-5'-phosphate conserved domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
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
induces copper regulated promoter, upregulates LctO 17fold (2D gel)
additional information
additional information
Zn2+, Fe2+, Ni2+, Mn2+, and Ca2+ have no significant effect on lctO expression
additional information
-
Zn2+, Fe2+, Ni2+, Mn2+, and Ca2+ have no significant effect on lctO expression
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoisocaproate
-
non-competitive inhibition at 5 mM, most active inhibitor of 2-keto acids, oxidation of 2-hydroxybutyrate most sensitive
3-decyl-2,5-dioxo-4-hydroxy-3-pyrroline
-
bound to the active site in the three-dimensional structure
4-carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole
-
bound to the active site in the three-dimensional structure
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
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
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
DL-2-hydroxy-3-butynoate
-
irreversible inactivation after 25 turnovers, covalent addition to the coenzyme
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
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
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-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-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-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'-(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-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
35% inhibition at 0.010 mM
4-chloromercuribenzoate
-
long chain oxidase, 29-42% inhibition at 0.001 mM, short chain oxidase: 70-75% inhibition at 0.001 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'-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-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-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-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-(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-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
iodoacetate
-
long chain oxidase, 31-36% inhibition at 0.1 mM, short chain oxidase: no inhibition
KCN
-
30% inhibition of L-2-hydroxyisocaproate oxidation at 1 mM, 91% inhibition of glycolate oxidation at 1 mM
o-Iodosobenzoate
-
long chain oxidase, 95-100% inhibition at 0.1 mM, short chain oxidase: no inhibition
oxalate
-
mixed-type non-competitive inhibition, increasing inhibitory effects as the number of carbons in aliphatic chains decreases
oxalate
-
18% inhibition of glycolate oxidation, 71% inhibition of glyoxylate oxidation at 0.03 mM
phosphate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
additional information
-
development of selective inhibitors of Hao2 from screening of a compound library, overview
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arsenate
-
increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
phosphate
-
increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
(s)-2-hydroxy-acid oxidase deficiency
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Adenocarcinoma
Cellular mechanism of resistance of human colorectal adenocarcinoma cells against apoptosis-induction by Russell's Viper venom l-amino acid oxidase (Rusvinoxidase).
Adenocarcinoma
In vitro cytotoxicity of L-amino acid oxidase from the venom of Crotalus mitchellii pyrrhus.
Adenocarcinoma
The toxin BjussuLAAO-II induces oxidative stress and DNA damage, upregulates the inflammatory cytokine genes TNF and IL6, and downregulates the apoptotic-related genes BAX, BCL2 and RELA in human Caco-2 cells.
Breast Neoplasms
Apoptosis induction in human breast cancer (MCF-7) cells by a novel venom L-amino acid oxidase (Rusvinoxidase) is independent of its enzymatic activity and is accompanied by caspase-7 activation and reactive oxygen species production.
Carcinoma
Electrochemical immunosensor based on chitosan-gold nanoparticle/carbon nanotube as a ?platform and lactate oxidase as a ?label for detection of CA125 oncomarker?.
Colonic Neoplasms
Cytotoxic, Anti-Proliferative and Apoptosis Activity of l-Amino Acid Oxidase from Malaysian Cryptelytrops purpureomaculatus (CP-LAAO) Venom on Human Colon Cancer Cells.
Colonic Neoplasms
Cytotoxic, Antiproliferative and Apoptosis-inducing Activity of L-Amino Acid Oxidase from Malaysian Calloselasma rhodostoma on Human Colon Cancer Cells.
Colonic Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Colorectal Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Colorectal Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Congenital Hyperinsulinism
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Dehydration
Nitrogen Metabolism in Adaptation of Photosynthesis to Water Stress in Rice Grown under Different Nitrogen Levels.
Edema, Cardiac
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Endometrial Neoplasms
Fraxetin inhibits the proliferation of RL95-2 cells through regulation of metabolism.
Fibrosarcoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Glioma
L-amino acid oxidase (LOX) modulation of melphalan activity against intracranial glioma.
Hyperoxaluria
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Hyperoxaluria
Potential mechanisms of marked hyperoxaluria not due to primary hyperoxaluria I or II.
Hyperoxaluria, Primary
An Investigational RNAi Therapeutic Targeting Glycolate Oxidase Reduces Oxalate Production in Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type I.
Hyperoxaluria, Primary
CRISPR/Cas9-mediated metabolic pathway reprogramming in a novel humanized rat model ameliorates primary hyperoxaluria type 1.
Hyperoxaluria, Primary
Dual Glycolate Oxidase/Lactate Dehydrogenase A Inhibitors for Primary Hyperoxaluria.
Hyperoxaluria, Primary
Glycolate Oxidase Is a Safe and Efficient Target for Substrate Reduction Therapy in a Mouse Model of Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Hyperoxaluria, Primary
High throughput cell-based assay for identification of glycolate oxidase inhibitors as a potential treatment for Primary Hyperoxaluria Type 1.
Hyperoxaluria, Primary
Inhibition of Glycolate Oxidase With Dicer-substrate siRNA Reduces Calcium Oxalate Deposition in a Mouse Model of Primary Hyperoxaluria Type 1.
Hyperoxaluria, Primary
Metabolism of (13)C5-hydroxyproline in mouse models of Primary Hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase.
Hyperoxaluria, Primary
Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Beta-lyase Plays in Hyperoxaluria.
Hyperoxaluria, Primary
Re: An Investigational RNAi Therapeutic Targeting Glycolate Oxidase Reduces Oxalate Production in Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
Re: CRISPR/Cas9-Mediated Glycolate Oxidase Disruption is an Efficacious and Safe Treatment for Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
Re: Glycolate Oxidase is a Safe and Efficient Target for Substrate Reduction Therapy in a Mouse Model of Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
Therapeutic RNA interference: A novel approach to the treatment of primary hyperoxaluria.
Infections
Expression profile of the fish immune enzyme l-amino acid oxidase (LAAO) after Streptococcus agalactiae infection in zebrafish (Danio rerio).
Infections
l-amino acid oxidase expression profile and biochemical responses of rabbitfish (Siganus oramin) after exposure to a high dose of Cryptocaryon irritans.
Kidney Calculi
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
Kidney Calculi
Purification and characterization of recombinant human liver glycolate oxidase.
Kidney Failure, Chronic
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Leukemia
Cytotoxic proteins of Amanita virosa Secr. mushroom: purification, characteristics and action towards mammalian cells.
Melanoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Myotoxicity
Combined venomics, antivenomics and venom gland transcriptome analysis of the monocoled cobra (Naja kaouthia) from China.
Neoplasms
Antiproliferative Activity of King Cobra (Ophiophagus hannah) Venom l-Amino Acid Oxidase.
Neoplasms
CR-LAAO, an L-amino acid oxidase from Calloselasma rhodostoma venom, as a potential tool for developing novel immunotherapeutic strategies against cancer.
Neoplasms
Dual-Modal Therapeutic Role of the Lactate Oxidase-Embedded Hierarchical Porous Zeolitic Imidazolate Framework as a Nanocatalyst for Effective Tumor Suppression.
Neoplasms
Intra/Extracellular Lactic Acid Exhaustion for Synergistic Metabolic Therapy and Immunotherapy of Tumors.
Neoplasms
Isolation, characterization and screening of the in vitro cytotoxic activity of a novel L-amino acid oxidase (LAAOcdt) from Crotalus durissus terrificus venom on human cancer cell lines.
Neoplasms
King cobra (Ophiophagus hannah) venom L-amino acid oxidase induces apoptosis in PC-3 cells and suppresses PC-3 solid tumor growth in a tumor xenograft mouse model.
Neoplasms
l-Amino acid oxidase from Cerastes vipera snake venom: Isolation, characterization and biological effects on bacteria and tumor cell lines.
Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Neoplasms
l-Amino acid oxidase isolated from Calloselasma rhodostoma snake venom induces cytotoxicity and apoptosis in JAK2V617F-positive cell lines.
Neoplasms
Openwork@Dendritic Mesoporous Silica Nanoparticles for Lactate Depletion and Tumor Microenvironment Regulation.
Neoplasms
Oxidoreductase activities in normal rat liver, tumor-bearing rat liver, and hepatoma HC-252.
Neoplasms
Peroxisome inspired hybrid enzyme nanogels for chemodynamic and photodynamic therapy.
Neoplasms
Repolarization of M2 to M1 macrophages triggered by lactate oxidase released from methylcellulose hydrogel.
Neoplasms
Targeting Tumor Microenvironment by Bioreduction-Activated Nanoparticles for Light-Triggered Virotherapy.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
L-amino acid oxidase isolated from Micrurus mipartitus snake venom (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia cells mostly via oxidative stress-dependent signaling mechanism.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
L-amino acid oxidase isolated from Micrurus mipartitus snake venom (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia cells mostly via oxidative stress-dependent signaling mechanism.
Pulmonary Edema
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Stomach Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Thrombocytopenia
Comparative proteomes, immunoreactivities and neutralization of procoagulant activities of Calloselasma rhodostoma (Malayan pit viper) venoms from four regions in Southeast Asia.
Unconsciousness
Danger in the Canopy. Comparative Proteomics and Bioactivities of the Venoms of the South American Palm Pit Viper Bothrops bilineatus Subspecies bilineatus and smaragdinus and Antivenomics of B. b. bilineatus (Rondônia) Venom against the Brazilian Pentabothropic Antivenom.
Urolithiasis
Experimental urolithiasis : Part II--a comparative kinetic study of glyoxalase I, glycolate oxidase, alkaline phosphatase & lactate dehydrogenase in the normal rat kidney & bladder & its alterations in urolithiasis.
Uterine Cervical Neoplasms
ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells.
Virus Diseases
Barley Stripe Mosaic Virus ?b Interacts with Glycolate Oxidase and Inhibits Peroxisomal ROS Production to Facilitate Virus Infection.
Vitamin B 6 Deficiency
Vitamin B6 deficiency as related to oxalate-synthesizing enzymes in growing rats.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
25.5
(S)-lactate
-
25°C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
47.6
(S)-lactate
-
35°C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
1.34
DL-2-hydroxycaproate