1.1.3.15: (S)-2-hydroxy-acid oxidase
This is an abbreviated version!
For detailed information about (S)-2-hydroxy-acid oxidase, go to the full flat file.
Word Map on EC 1.1.3.15
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1.1.3.15
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venom
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snake
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catalase
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biosensors
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laaos
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electrode
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glyoxylate
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oxidases
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electrochemical
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amperometric
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photorespiration
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oxalate
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photorespiratory
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bothrops
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d-amino
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crotalus
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hyperoxalurias
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viper
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antivenoms
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hydroxypyruvate
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microbodies
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snakebite
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crisp
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calloselasma
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cobra
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rhodostoma
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trimeresurus
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thrombin-like
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glyoxysomes
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agkistrodon
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kaouthia
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rattlesnake
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viridans
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adamanteus
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screen-printed
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flavocytochrome
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malayan
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elapid
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fmn-dependent
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phosphomonoesterase
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svmps
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viperids
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hannah
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l-leu
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aerococcus
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daboia
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atrox
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drug development
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diagnostics
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medicine
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synthesis
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bradykinin-potentiating
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analysis
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molecular biology
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three-finger
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agriculture
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nafion
- 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
Reaction
Synonyms
(L)-2-HAOX, (S)-2-hydroxy-acid oxidase, peroxisomal, 2-hydroxy acid oxidase, CSUB_C1080, EC 1.1.3.1, GLO, Glo1, GLO3, Glo4, glycolate oxidase, GO, GO1, GOX, GOX1, GOX2, HAO1, Hao2, HAOX, HAOX1, HAOX2, HAOX3, hydroxy-acid oxidase A, hydroxy-acid oxidase B, hydroxyacid oxidase 1, hydroxyacid oxidase A, L-2-hydroxy acid oxidase, L-2-hydroxyacid oxidase A, L-alpha-hydroxy acid oxidase, L-amino acid oxidase, L-LAC-OX, L-lactate monooxygenase, L-lactate oxidase, L-LOx, lactate oxidase, LCHAO, LctO, lHAOX1, lHAOX2, long chain hydroxy acid oxidase, long chain l-2-hydroxy acid oxidase, long chain L-2-hydroxy acid oxidase 2, long-chain 2-hydroxy acid oxidase, long-chain L-alpha-hydroxy acid oxidase, LOX, More, NbS00005125g0015, NbS00060838g0004, Nbv5tr6245008, Os03g0786100, Os04g0623500, Os07g0616500, oxidase, L-2-hydroxy acid, RCOM_0631490, RCOM_0684800
ECTree
1.1.3.15 (S)-2-hydroxy-acid oxidaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A95G
E160G/V198I
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the half-life of the mutant lactate oxidase at 70°C is about 18times that of the wild-type enzyme. Km-value for (S)-lactate at 25°C is 46fold higher than wild-type value, Km-value for (S)-lactate at 25°C is 59fold higher than wild-type value
E160G/V198I/G36S/T103S/A232S/F277Y
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the half-life of the mutant lactate oxidase at 70°C is about 2 times that of E160G/V198I mutant and about 36 times that of the wild-type enzyme. Km-value for (S)-lactate at 25°C is 48fold higher than wild-type value, Km-value for (S)-lactate at 25°C is 55fold higher than wild-type value. Mutant is obtained by direct evolution
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
A95G
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much enhanced oxidase activity with longer chain L-alpha-hydroxyacids such as alpha-hydroxy-n-butyric acid, alpha-hydroxy-n-valeric acid and L-mandelic acid
A95G
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enhanced activity with bulky substrates, increase in the reduction rate constants with substrates having a bulky alpha-substituent such as mandelate, when compared with wild-type enzyme
additional information
Arabidopsis thaliana plants overexpressing glycolate oxidase in chloroplasts accumulates both hydrogen peroxide and glyoxylate, enzyme-overexpressing plants show retarded development, yellowish rosettes, and impaired photosynthetic performance. The plants develop oxidative stress lesions under photorespiratory conditions but grow like wild-type plants under nonphotorespiratory conditions, phenotype, 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
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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
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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
additional information
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Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
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additional information
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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
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additional information
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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
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additional information
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co-expression of GOX with capsid protein P8 targets capsid protein P8 into peroxisomes: time course analysis demonstrates that the localization of capsid protein P8 in peroxisomes of Spodoptera frugiperda cells, co-expressing capsid protein P8 and GOX, changes from diffuse to discrete, punctuate inclusions during expression from 24 to 48 h post inoculation
additional information
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yeast two-hybrid and co-immunoprecipitation assays indicate that capsid protein P8, an outer capsid protein of Rice dwarf phytoreovirus (RDV), interacts with rice glycolate oxidase (GOX)
additional information
phenotypes of GLO-suppressed plants under air and high CO2, overview. The plants with 30%, 60%, and 90% reduced GLO activities accumulate 40, 60, and 130fold, respectively, more glycolate than the wild-type
additional information
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phenotypes of GLO-suppressed plants under air and high CO2, overview. The plants with 30%, 60%, and 90% reduced GLO activities accumulate 40, 60, and 130fold, respectively, more glycolate than the wild-type
additional information
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construction and evaluation of a biosensor of chiral, biocompatible, conducting material comprising collagen I, silica gel and ferrocene involving glucose oxidase/lactate oxidase enzymes. Preparation of the ferrocene/collagen or ferrocene/collagen/silica modified electrodes. The material modifies and inverts the chiral selectivity of D-glucose oxidase and L-lactate oxidase in collagen incorporated in tetramethoxysilane, overview
additional information
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immobilization of the enzyme from water-organic solvent mixture on biosensor membranes, most active enzyme containing membranes are obtained using triethoxysiloxanes: gamma-aminopropyl-,vinyl-, or phenyl-triethoxysiloxane, method optimization and evaluation, overview. Lactate oxidase remains with more than 60% of it is initial activity after exposing to water-isopropanol mixtures with over 90% v/v content of organic solvent
additional information
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imobilization of the enzyme on gold electrodes, determination of lactate oxidase patterns with gold substrates, in terms of homogeneity, compactness and stability, overview. LOx is directly stamped to a bare gold surface, LOx is previously covalently bonded to a thiolated molecule, dithiodipropionic acid di-N-succinimidyl ester, and this conjugate is transferred from an elastomeric stamp to a bare gold substrate, formation of a LOx/DTSP micropattern on a bare gold surface, which is followed by exposure to a solution containing hexadecylmercaptane
additional information
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
additional information
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Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
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additional information
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in an enzyme disruption mutant, the highest concentration of H2O2 attained in the medium is found to be approximately 1 mM, about one-fifth the level for the parental strain. Although cell growth continuous until glucose in the medium becomes undetectable even in the absence of added catalase, the maximum cell mass attained is considerably higher in the presence of catalase than in its absence. The maximum cell mass achieved in the presence of added catalase is reproducibly lower by 0.2 to 0.3 turbidity units than that of the parent
additional information
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in an enzyme disruption mutant, the highest concentration of H2O2 attained in the medium is found to be approximately 1 mM, about one-fifth the level for the parental strain. Although cell growth continuous until glucose in the medium becomes undetectable even in the absence of added catalase, the maximum cell mass attained is considerably higher in the presence of catalase than in its absence. The maximum cell mass achieved in the presence of added catalase is reproducibly lower by 0.2 to 0.3 turbidity units than that of the parent
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