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Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase and Organism(s) Oryza sativa and UniProt Accession Q10CE4
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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
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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: Oryza sativa
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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glycolate oxidase
GOX
HAOX1
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HAOX2
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HAOX3
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hydroxy-acid oxidase A
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hydroxy-acid oxidase B
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hydroxyacid oxidase A
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L-2-hydroxy acid oxidase
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L-alpha-hydroxy acid oxidase
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oxidase, L-2-hydroxy acid
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glycolate oxidase
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GOX
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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oxidative decarboxylation
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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
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
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
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
?
-
-
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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confocal immunofluorescence microscopy reveals that capsid protein P8 is colocalized with GOX in peroxisomes
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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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)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of at least five putative GLO gene members in the rice genome, which are located on chromosome 3, 4, and 7, respectively
co-expression of the enzyme with the Rice dwarf virus, RDV, outer capsid P8 protein in Spodoptera frugiperda cells, the localization of P8 in Spodoptera frugiperda cells changed from diffuse to discrete, punctuate inclusions during expression from 24 to 48 h post inoculation, coexpression of GOX with P8 may target P8 into peroxisomes, which serve as replication sites for a number of viruses
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the suppression effect of estradiol is dependent on the concentration of estradiol. A reduction of about 60% is observed when 0.001 mM estradiol is applied for 10 d, and the maximal reduction of over 90% occurs at 0.005 mM
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
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the interaction of capsid protein P8 with the GOX of host cells leads to translocation of capsid protein P8 into peroxisomes. The interaction between capsid protein P8 and GOX plays important roles in Rice dwarf phytoreovirus targeting into the replication site of host cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, W.J.; Huang, J.Q.; Yang, C.; Huang, J.J.; Li, M.Q.
The recognition of glycolate oxidase apoprotein with flavin analogs in higher plants
Acta Biochim. Biophys. Sin.
36
290-296
2004
Brassica rapa subsp. oleifera, Carica papaya, Cucumis sativus, Nicotiana tabacum, Oryza sativa, Spinacia oleracea, Triticum aestivum, Vigna unguiculata, Zea mays
Zhou, F.; Wu, G.; Deng, W.; Pu, Y.; Wei, C.; Li, Y.
Interaction of rice dwarf virus outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8
FEBS Lett.
581
34-40
2007
Oryza sativa
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