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Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase and Organism(s) Rattus norvegicus and UniProt Accession Q07523
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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: Rattus norvegicus
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
-
-
-
-
glycolate oxidase
-
-
-
-
GOX
-
-
-
-
HAOX1
-
-
-
-
HAOX2
-
-
-
-
HAOX3
-
-
-
-
hydroxy-acid oxidase A
-
-
-
-
hydroxy-acid oxidase B
-
-
-
-
hydroxyacid oxidase A
-
-
-
-
L-2-hydroxy acid oxidase
L-alpha-hydroxy acid oxidase
-
-
-
-
oxidase, L-2-hydroxy acid
-
-
-
-
additional information
the enzyme belongs to the FMN-dependent enzyme family
L-2-hydroxy acid oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
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
-
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
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
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
-
-
?
additional information
?
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
?
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
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
additional information
?
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-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-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-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-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
35% inhibition at 0.010 mM
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0012
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0107
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0006
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0005
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0002
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0011
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0017
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0007
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0013
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0013
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0357
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.002
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0011
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.048
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0009
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0076
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0005
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0002
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0358
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0137
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
11
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0407
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0339
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0007
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00135
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0091
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0009
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0005
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0002
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0011
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0217
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0009
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0009
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0318
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00091
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0008
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0005
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0018
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
decrease of enzyme activity upon oxidative stress induced by glutathione depletion or postischemic perfusion
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Hao2 is highly significantly downregulated in 12/12 HCCs developed by the CMD protocol and in 16/16 HCCs generated by chronic DENA treatment
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular localization analysis, no enzyme activity in cytosol, mitochondrial membrane, or mitochondrial matrix, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the family of L-2-hydroxy acid oxidases
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
-
pharmacological role of the enzyme in the management of blood pressure
additional information
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
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). HAOX2_RAT
353
0
39201
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structure analysis, modelling, the enzyme shows the same beta8alpha8 TIM barrel structure as other structurally characterized family members of the FMN-dependent enzyme family
additional information
-
molecular modeling studies using the rat Hao2 crystal structure, PDB ID 1TB3, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structure of enzyme LCHAO in complex with cofactor FMN and inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole (CCPST) at 1.3 A resolution
sitting drop vapor diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein in 0.1 M Tris, pH 7.5, mixed with the same volume of reservoir solution containing 0.4 M sodium acetate and 0.2 M sodium citrate, pH 6.5, equilibration at 4°C, soaking of crystals in 25% glycerol-containing reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y129F
site-directed mutagenesis of the key active site residue, the mutant enzymes shows highly reduced kcat but unaltered Km value compared to wild-type enzyme, modeling of the hydride transfer of mutant enzyme with bound FMN and lactate, the missing H-bond changes the mechanism of the LCHAO Y129F mutant catalyzed oxidation reaction
additional information
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography to high purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Hao2, isozymes beta1 and beta2, cloning from kidney, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) using vector pET28a
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
drug development
-
isozyme Hao2 is a target for drug development in high blood pressure
medicine
-
decrease of enzyme activity upon oxidative stress induced by glutathione depletion or postischemic perfusion, down-regulation of enzyme as mechanism to prevent excessive H2O2 formation in liver peroxisome
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Recalcati, S.; Tacchini, L.; Alberghini, A.; Conte, D.; Cairo, G.
Oxidative stress-mediated down-regulation of rat hydroxyacid oxidase 1, a liver-specific peroxisomal enzyme
Hepatology
38
1159-1166
2003
Rattus norvegicus
Cunane, L.M.; Barton, J.D.; Chen, Z.W.; Le, K.H.; Amar, D.; Lederer, F.; Mathews, F.S.
Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase
Biochemistry
44
1521-1531
2005
Rattus norvegicus (Q07523)
de Bari, L.; Valenti, D.; Atlante, A.; Passarella, S.
L-lactate generates hydrogen peroxide in purified rat liver mitochondria due to the putative L-lactate oxidase localized in the intermembrane space
FEBS Lett.
584
2285-2290
2010
Rattus norvegicus
Barawkar, D.; Meru, A.; Bandyopadhyay, A.; Banerjee, A.; Deshpande, A.; Athare, C.; Koduru, C.; Khose, G.; Gundu, J.; Mahajan, K.; Patil, P.; Kandalkar, S.; Niranjan, S.; Bhosale, S.; De, S.; Mukhopadhyay, S.; Chaudhary, S.; Koul, S.; Singh, U.; Chugh, A.
Potent and selective inhibitors of long chain l-2-hydroxy acid oxidase reduced blood pressure in DOCA salt-treated rats
ACS Med. Chem. Lett.
2
919-923
2011
Rattus norvegicus
Barawkar, D.A.; Bandyopadhyay, A.; Deshpande, A.; Koul, S.; Kandalkar, S.; Patil, P.; Khose, G.; Vyas, S.; Mone, M.; Bhosale, S.; Singh, U.; De, S.; Meru, A.; Gundu, J.; Chugh, A.; Palle, V.P.; Mookhtiar, K.A.; Vacca, J.P.; Chakravarty, P.K.; Nargund, R.P.; Wright, S.D.; Roy, S.; Graziano, M.P.; Cully, D.; Ca, C.a.i.
Discovery of pyrazole carboxylic acids as potent inhibitors of rat long chain L-2-hydroxy acid oxidase
Bioorg. Med. Chem. Lett.
22
4341-4347
2012
Homo sapiens, Rattus norvegicus
Su, C.; Yu, L.; Yao, T.; Zeng, S.
Cloning and expression of recombinant rat long-chain 2-hydroxy acid oxidase
Chin. Pharmaceut. J.
48
331-336
2013
Rattus norvegicus (Q07523)
-
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)
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