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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
-
biosensors
-
electrode
- laaos
-
amperometric
-
electrochemical
-
oxidases
- bothrops
-
d-amino
- hyaluronidase
- cobra
- rhodostoma
-
antivenoms
- crotalus
- calloselasma
-
phosphomonoesterase
- pitviper
- trimeresurus
- kaouthia
-
crisp
- adamanteus
-
viperid
- viridans
- l-leu
-
elapid
-
malayan
-
fmn-dependent
- hannah
-
snakebite
-
thrombin-like
- rattlesnake
- aerococcus
-
myotoxic
-
nafion
-
screen-printed
-
ophiophagus
- l-phe
-
l-lactic
- agkistrodon
- daboia
-
svmps
- molecular biology
- diagnostics
- jararaca
-
bradykinin-potentiating
- halys
- analysis
- atrox
- drug development
- synthesis
-
2-monooxygenase
-
three-finger
- medicine
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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
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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
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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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-
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redox reaction
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-
-
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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
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-
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287560, 389680, 389685, 389686, 389687, 389688, 389689, 389690, 389691, 389692, 389693, 389694, 389698, 389700, 389703
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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
A9QH71
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
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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
A9QH71
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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the enzyme belongs to the family of L-2-hydroxy acid oxidases
evolution
enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. Vertebrates possess lHAOX proteins acting on similar substrates as plant lHAOX. The existence of GOX and lHAOX subfamilies in both plants and animals is not due to shared ancestry but is the result of convergent evolution in the two most complex eukaryotic lineages. Duplication and diversification occurred independently at the base of deuterostomia and at the base of vascular plants. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview. Convergent evolution in vascular plants and deuterostomia; enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. Vertebrates possess lHAOX proteins acting on similar substrates as plant lHAOX. The existence of GOX and lHAOX subfamilies in both plants and animals is not due to shared ancestry but is the result of convergent evolution in the two most complex eukaryotic lineages. Duplication and diversification occurred independently at the base of deuterostomia and at the base of vascular plants. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview. Convergent evolution in vascular plants and deuterostomia; enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). The encoding gene is thought to have originated from endosymbiotic gene transfer between the eukaryotic host and the cyanobacterial endosymbiont at the base of plantae. Animals also possess GOX activities. Plant and animal GOX belong to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview
evolution
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the enzyme belongs to the family of L-2-hydroxy acid oxidases
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malfunction
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the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
malfunction
-
evaluation of the potential of siRNAs targeting the synthesis of liver glycolate oxidase or hydroxyproline dehydrogenase formulated in lipid nanoparticles, to reduce urinary oxalate excretion in Agxt KO mice. The siRNA targeting glycolate oxidase blocks a downstream step and prevents the synthesis of glyoxylate from glycolate in the liver. The ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans
malfunction
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an alternative approach to prevent glyoxylate production in subjects with primary hyperoxaluria type 1 (PH1) is using Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, which encodes glycolate oxidase (GO), to reduce the hepatic conversion of glycolate to glyoxylate. This approach efficiently reduces GO mRNA and protein in the livers of mice. Reduction of hepatic GO leads to normalization of urine oxalate levels and reduces CaOx deposition in a preclinical mouse model of PH1. Hao1-/- mice show elevated levels of urinary glycolate without renal damage or other phenotypic consequences
malfunction
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an alternative approach to prevent glyoxylate production in subjects with primary hyperoxaluria type 1 (PH1) is using Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, which encodes glycolate oxidase (GO), to reduce the hepatic conversion of glycolate to glyoxylate. This approach efficiently reduces GO mRNA and protein in the livers of mice. Reduction of hepatic GO leads to normalization of urine oxalate levels and reduces CaOx deposition in a preclinical mouse model of PH1. Hao1-/- mice show elevated levels of urinary glycolate without renal damage or other phenotypic consequences
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malfunction
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evaluation of the potential of siRNAs targeting the synthesis of liver glycolate oxidase or hydroxyproline dehydrogenase formulated in lipid nanoparticles, to reduce urinary oxalate excretion in Agxt KO mice. The siRNA targeting glycolate oxidase blocks a downstream step and prevents the synthesis of glyoxylate from glycolate in the liver. The ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans
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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
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the enzyme performs an essential step in the operation of the oxidative photorespiratory cycle accompanying photosynthetic CO2 assimilation in C3 plants
physiological function
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role in C3 and C4 plants and associated regulation mechanisms
physiological function
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role in C3 and C4 plants and associated regulation mechanisms
physiological function
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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
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
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L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
glycolate oxidase (GOX) is a crucial enzyme of plant photorespiration
physiological function
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L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
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physiological function
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L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
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additional information
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the key residue Tyr129 in the active site of LCHAO does affect L-lactate binding to LCHAO but plays an important role on the catalytic reaction process through an H-bond interaction. Generation of a structural model of LCHAO-FMN-lactate. The active site informed by residues Phe23, Tyr129, Asp157, Arg164, Lys223, His247, and Arg250
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX; structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX; structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX; structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX; structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX; structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX; structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
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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 + ?
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transhydrogenation reaction
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?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
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-
-
?
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
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r
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
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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
-
?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
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70% of the activity compared to DL-2-hydroxybutyrate
-
?
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
-
-
-
?
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
-
-
?
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
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90% of the activity compared to DL-2-hydroxybutyrate
-
?
glycolate + 2,4-dinitrophenylhydrazine
glyoxylate 2,4-dinitrophenylhydrazone
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best substrate tested
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
glycolate + phenazine methosulfate
glyoxylate + reduced phenazine methosulfate
-
-
-
?
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
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
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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
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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 + 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
?
-
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 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
?
-
-
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 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-hydroxycaproate + O2
2-oxocaproate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
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
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q9WU19
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q07523
-
-
-
?
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
?
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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additional information
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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
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increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
phosphate
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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