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Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LRR9
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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: Arabidopsis thaliana
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
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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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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
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
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-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
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-
-
?
2-hydroxydodecanoate + O2
2-oxododecanoate + H2O2
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-
-
?
2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
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-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
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-
-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
additional information
?
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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
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?
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
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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
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE 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
evolution
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
physiological function
glycolate oxidase (GOX) is a crucial enzyme of plant photorespiration
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
metabolism
the enzyme is involved in the glyoxylate metabolism, overview
additional information
additional information
structure homology modeling of Arabidopsis thaliana GOX1 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
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
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 lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
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). GLO1_ARATH
367
0
40341
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 39900, recombinant enzyme without tag, SDS-PAGE
?
x * 40100, recombinant enzyme without tag, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BLR DE3 pLysS by nickel affinity chromatography and desalting gel filtration to homogeneity
recombinant His-tagged enzyme from Escherichia coli strain BLR(DE3) pLysS by nickel affinity chromatography and desalting gel filtration to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes Glo1, sequence comparisons, phylogenetic analysis and tree
genes Glo3, sequence comparisons, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR (DE3) pLysS
genes Glo4, sequence comparisons, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR DE3 pLysS
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fahnenstich, H.; Scarpeci, T.E.; Valle, E.M.; Fluegge, U.I.; Maurino, V.G.
Generation of hydrogen peroxide in chloroplasts of Arabidopsis overexpressing glycolate oxidase as an inducible system to study oxidative stress
Plant Physiol.
148
719-729
2008
Arabidopsis thaliana (Q56ZN0)
Esser, C.; Kuhn, A.; Groth, G.; Lercher, M.J.; Maurino, V.G.
Plant and animal glycolate oxidases have a common eukaryotic ancestor and convergently duplicated to evolve long-chain 2-hydroxy acid oxidases
Mol. Biol. Evol.
31
1089-1101
2014
Arabidopsis thaliana (Q24JJ8), Arabidopsis thaliana (Q9LJH5), Arabidopsis thaliana (Q9LRR9)
EXTERNAL LINKS (specific for EC-Number 1.1.3.15)
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