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Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase and Organism(s) Mus musculus and UniProt Accession Q9WU19
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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 taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
l-amino acid oxidase, glycolate oxidase, lactate oxidase, haox1, l-alpha-hydroxy acid oxidase, l-2-hydroxy acid oxidase, lchao, l-lactate monooxygenase, hydroxyacid oxidase 1, (l)-2-haox, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-2-hydroxy-acid oxidase, peroxisomal
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-
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glycolate oxidase
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-
-
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GOX
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-
-
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HAOX1
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-
-
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HAOX2
-
-
-
-
HAOX3
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-
-
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hydroxy-acid oxidase A
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-
-
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hydroxy-acid oxidase B
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-
-
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hydroxyacid oxidase A
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-
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L-2-hydroxy acid oxidase
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-
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L-alpha-hydroxy acid oxidase
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-
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oxidase, L-2-hydroxy acid
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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oxidative decarboxylation
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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.
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
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
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substrate for isoenzyme B
-
?
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
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
malfunction
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HAOX1_MOUSE
370
0
41001
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme knockout by Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, relationship of Hao1 mRNA and glycolate oxidase protein knockdown to oxalate reduction, overview
additional information
-
enzyme knockout by Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, relationship of Hao1 mRNA and glycolate oxidase protein knockdown to oxalate reduction, overview
additional information
enzyme knockout by specific siRNA targeting the liver enzyme glycolate oxidase in wild-type leads to greatly decreased GO activity, 20fold increased urinary excretion of glycolate, and more than 2fold increased urinary oxalate excretion compared to controls. Treatment of mutant Agxt KO mice, that are deficient in liver alanine:glyoxylate aminotransferase, leads to significantly decreased urinary oxalate excretion, but substantially increased urinary glycolate excretion
additional information
-
enzyme knockout by specific siRNA targeting the liver enzyme glycolate oxidase in wild-type leads to greatly decreased GO activity, 20fold increased urinary excretion of glycolate, and more than 2fold increased urinary oxalate excretion compared to controls. Treatment of mutant Agxt KO mice, that are deficient in liver alanine:glyoxylate aminotransferase, leads to significantly decreased urinary oxalate excretion, but substantially increased urinary glycolate excretion
additional information
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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, genes HYPDH and GO appear to be the best targets for reducing the production of glyoxylate and oxalate in PH patients
medicine
application of oan in vivo CRISPR/Cas9-mediated substrate reduction therapy to treat primary hyperoxaluria type I that results in excessive hepatic oxalate production causing end-stage renal disease. A single systemic administration of an AAV8-CRISPR/Cas9 vector targeting glycolate oxidase, prevents oxalate overproduction and kidney damage, with no signs of toxicity in Agxt1-/- mice
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duley, J.A.; Holmes, R.S.
L-alpha-hydroxyacid oxidase isozymes. Purification and properties
Eur. J. Biochem.
63
163-173
1976
Mus musculus, Rattus sp.
Li, X.; Knight, J.; Fargue, S.; Buchalski, B.; Guan, Z.; Inscho, E.W.; Liebow, A.; Fitzgerald, K.; Querbes, W.; Todd Lowther, W.; Holmes, R.P.
Metabolism of (13)C5-hydroxyproline in mouse models of primary hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase
Biochim. Biophys. Acta
1862
233-239
2016
Mus musculus (Q9WU19), Mus musculus, Mus musculus C57BL/6J (Q9WU19)
Mattu, S.; Fornari, F.; Quagliata, L.; Perra, A.; Angioni, M.M.; Petrelli, A.; Menegon, S.; Morandi, A.; Chiarugi, P.; Ledda-Columbano, G.M.; Gramantieri, L.; Terracciano, L.; Giordano, S.; Columbano, A.
The metabolic gene HAO2 is downregulated in hepatocellular carcinoma and predicts metastasis and poor survival
J. Hepatol.
64
891-898
2016
Rattus norvegicus (Q07523), Mus musculus (Q9NYQ2), Homo sapiens (Q9NYQ3), Mus musculus C3H (Q9NYQ2), Rattus norvegicus Fischer 344 (Q07523)
Dutta, C.; Avitahl-Curtis, N.; Pursell, N.; Larsson Cohen, M.; Holmes, B.; Diwanji, R.; Zhou, W.; Apponi, L.; Koser, M.; Ying, B.; Chen, D.; Shui, X.; Saxena, U.; Cyr, W.A.; Shah, A.; Nazef, N.; Wang, W.; Abrams, M.; Dudek, H.; Salido, E.; Brown, B.D.; Lai, C.
Inhibition of glycolate oxidase with dicer-substrate siRNA reduces calcium oxalate deposition in a mouse model of primary hyperoxaluria type 1
Mol. Ther.
24
770-778
2016
Mus musculus (Q9WU19), Mus musculus, Mus musculus C57BL/6 (Q9WU19)
Zabaleta, N.; Barberia, M.; Martin-Higueras, C.; Zapata-Linares, N.; Betancor, I.; Rodriguez, S.; Martinez-Turrillas, R.; Torella, L.; Vales, A.; Olaguee, C.; Vilas-Zornoza, A.; Castro-Labrador, L.; Lara-Astiaso, D.; Prosper, F.; Salido, E.; Gonzalez-Aseguinolaza, G.; Rodriguez-Madoz, J.R.
CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type I
Nat. Commun.
9
5454
2018
Mus musculus (Q9WU19)
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