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Enzyme Nomenclature
Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase
for references in articles please use BRENDA:EC1.1.3.15
Word Map on EC 1.1.3.15
- 1.1.3.15
- venom
- snake
- laaos
-
oxidases
-
d-amino
- bothrops
-
antivenoms
- cobra
- hyaluronidase
- crotalus
- calloselasma
- rhodostoma
-
phosphomonoesterase
-
malayan
-
crisp
-
aerococcus
- adamanteus
- l-leu
-
myotoxic
-
viperid
- rattlesnake
- kaouthia
-
fmn-dependent
-
snakebite
- viridans
- agkistrodon
- l-phe
-
ophiophagus
-
elapid
- trimeresurus
- hannah
-
thrombin-like
- pitviper
- halys
- synthesis
- molecular biology
- echis
- analysis
- jararaca
- daboia
-
three-finger
- medicine
-
bradykinin-potentiating
- drug development
- atrox
- diagnostics
-
svmps
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.3.15
-
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RECOMMENDED NAME
GeneOntology No.
(S)-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
-
-
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
correlation of enzyme activity with content of beta-N-oxalyl-L-alpha,beta-diaminopropionic acid under high light treatment
-
-
-
287560, 389680, 389685, 389686, 389687, 389688, 389689, 389690, 389691, 389692, 389693, 389694, 389698, 389700, 389703
-
-
type 2 lactate oxidase isolated from Strptococcus iniae; major pathogen of farmed fish, type 2 is an isolate from diseased barramundi (Lates calcarifer) in Northern Territory, Australia
UniProt
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
-
-
-
-
-
authors suggest a different annotation for the lctO gene with LctO translation starting at Met-18, encoding a protein of 366 amino acids
UniProt
authors suggest a different annotation for the lctO gene with LctO translation starting at Met-18, encoding a protein of 366 amino acids
UniProt
type 2 lactate oxidase isolated from Strptococcus iniae; major pathogen of farmed fish, type 2 is an isolate from diseased barramundi (Lates calcarifer) in Northern Territory, Australia
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
metabolism
physiological function
metabolism
the enzyme is involved in the glyoxylate metabolism, overview
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
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
-
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
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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
2-hydroxybutanoate + bromopyruvate + ?
bromolactate + pyruvate + ?
-
transhydrogenation reaction
-
?
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
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
DL-2-hydroxy-3-butynoate + O2
2-oxo-3-butynoate + H2O2
-
good substrate, but inactivation after 25 turnovers
-
?
DL-2-hydroxy-3-heptynoate + O2
2-oxo-3-heptynoate + H2O2
-
86% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-hexynoate + O2
2-oxo-3-hexynoate + H2O2
-
65% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
-
70% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-pentynoate + O2
2-oxo-3-pentynoate + H2O2
-
2fold higher activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-4-methylmercaptobutyrate + 2,6-dichlorophenolindophenol
2-oxo-4-methylmercaptobutyrate + reduced 2,6-dichlorophenolindophenol
-
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
-
-
-
?
DL-2-hydroxybutyrate + 2,4-dinitrophenylhydrazine
2-oxobutyrate 2,4-dinitrophenylhydrazone
-
low activity
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol
2-oxocaproate + reduced 2,6-dichlorophenolindophenol
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxydecanoate + 2,6-dichlorophenolindophenol
2-oxodecanoate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, traces of activity for short chain oxidase
-
?
DL-2-hydroxyisovalerate + 2,4-dinitrophenylhydrazine
2-oxoisovalerate 2,4-dinitrophenylhydrazone
-
very low activity
-
?
DL-2-hydroxyisovalerate + 2,6-dichlorophenolindophenol
2-oxoisovalerate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxooctanoate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol
2-oxovalerate + reduced 2,6-dichlorophenolindophenol
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-3-indolelactate + 2,6-dichlorophenolindophenol
3-indolepyruvate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-3-methoxy-4-hydroxymandelate + 2,6-dichlorophenolindophenol
(3-methoxy-4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-beta-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
DL-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
low activity
-
?
DL-mandelate + O2
phenylglyoxylic acid + H2O2
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol
(4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
DL-p-hydroxymandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
-
90% of the activity compared to DL-2-hydroxybutyrate
-
?
glycolate + 2,4-dinitrophenylhydrazine
glyoxylate 2,4-dinitrophenylhydrazone
-
best substrate tested
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
glycolate + phenazine methosulfate
glyoxylate + reduced phenazine methosulfate
B7FUG8
-
-
-
?
glyoxylate + 2,4-dinitrophenylhydrazine
oxalate 2,4-dinitrophenylhydrazone
-
25% of the activity compared to glycolate
-
?
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
-
?
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
-
-
-
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-4-chloromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-fluoromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methoxymandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methylmandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-nitromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-trifluoromethylmandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-lactate + 2,4-dinitrophenylhydrazine
pyruvate 2,4-dinitrophenylhydrazone
-
very low activity
-
?
L-lactate + phenazine methosulfate
? + reduced phenazine methosulfate
B7FUG8
-
-
-
?
L-leucine + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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
-
-
?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
may be the physiological substrates
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
glucose-repressible lactate oxidase is likely responsible for H2O2 production
-
-
?
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 + 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
-
?
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
-
?
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
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
-
the catalytic adduct is formed by hydrogen abstraction from the re-face of glycolate
-
-
?
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 + 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
-
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
?
-
-
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
?
-
B7FUG8
the enzyme is not able to metabolize D-lactate
-
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
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
-
?
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
?
-
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
?
-
Q19U05
the enzyme is involved in the photorespiration process
-
-
-
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
Zn2+, Fe2+, Ni2+, Mn2+, and Ca2+ have no significant effect on lctO expression
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INHIBITORS
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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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
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
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-Mentin kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE