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Information on EC 1.1.1.26 - glyoxylate reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LSV0
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1.1.1.26 glyoxylate reductaseIUBMB Comments
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
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Word Map
- 1.1.1.26
- hyperoxalurias
- oxalate
- ph2
- stone
- nephrolithiasis
- nephrocalcinosis
- l-glycerate
-
photorespiratory
-
alanine:glyoxylate
-
urolithiasis
- 4-hydroxy-2-oxoglutarate
- glyrs
- diagnostics
- medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
grhpr, glyoxylate reductase, glyr1, glyoxylate reductase/hydroxypyruvate reductase, glyr2, glyoxylate/hydroxypyruvate reductase, nadh-dependent glyoxylate reductase, nadh-glyoxylate reductase, glyoxylic acid reductase, succinic semialdehyde/glyoxylate reductase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycolate oxidase
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glyoxylic acid reductase
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NADH-dependent glyoxylate reductase
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NADH-glyoxylate reductase
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reductase, glyoxylate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -
SYSTEMATIC NAME
IUBMB Comments
glycolate:NAD+ oxidoreductase
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
CAS REGISTRY NUMBER
COMMENTARY
9028-32-4
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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
glyoxylate + NADPH
glycolate + NADP+
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a recombinant gamma hydroxybutyrate dehydrogenase, EC 1.1.1.61, exhibits high glyoxylate reductase activity with a 250fold higher preference for glyoxylate than with succinic semialdehyde, via an essentially irreversible, NADPH-based mechanism, overview
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ir
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
reaction of EC 1.1.1.29
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
reaction of EC 1.1.1.29, NADPH is a poor cofactor for wild-type
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-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
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succinic semialdehyde-dependent GLYR activity potentially occurs in planta, despite the fact that glyoxylate is the preferred substrate in vitro
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ir
additional information
?
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the enzyme prefers succinic semialdehyde 100fold to formaldehyde, acetaldehyde, butyraldehyde, 2-carboxybenzaldehyde, glyoxal, methylglyoxal, phenylglyoxal, and phenylglyoxylate
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?
additional information
?
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both cytosolic GLYR1 and plastidial GLYR2 catalyse the essentially irreversible, NADPH-based conversion of glyoxylate into glycolate, and can be regulated by the NADPH/NADP ratio
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?
additional information
?
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the recombinant AtHPR1 prefers prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
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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
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
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succinic semialdehyde-dependent GLYR activity potentially occurs in planta, despite the fact that glyoxylate is the preferred substrate in vitro
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-
ir
additional information
?
-
-
both cytosolic GLYR1 and plastidial GLYR2 catalyse the essentially irreversible, NADPH-based conversion of glyoxylate into glycolate, and can be regulated by the NADPH/NADP ratio
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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GLYR activity is found at all developmental stages and in all tissues, and activity is generally higher in vegetative and reproductive organs than in roots
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
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additional information
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GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
metabolism
physiological function
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succinic semialdehyde and glyoxylate are typically generated in leaves via two distinct metabolic pathways, 4-aminobutyrate and glycolate respectively. GLYR isozymes function in the detoxification of both aldehydes during stress and contribute to redox balance, overview
additional information
metabolism
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the enzyme is involved in the glycolate metabolism, as well as the 4-hydroxybutyrate production and the GABA shunt pathway, overview
metabolism
HPR1 phosphomimetic variant T335D exhibits reduced NADH-dependent hydroxypyruvate reductase activity but improved NADPH-dependent activity. Complementation of the Arabidopsis HPR1 mutant by either wild-type HPR1 or HPR1 nonphosphorylatable mutant T335A fully complements the photorespiratory growth phenotype of the HPR1 mutant in ambient air, whereas HPR1 T335D-containing HPR1 mutant plants remain smaller and have lower photosynthetic CO2 assimilation rates. These phenotypes were associated with subtle perturbations in the photorespiratory cycle of HPR1 T335D-complemented HPR1 mutant rosettes compared to all other HPR1-containing lines
additional information
due to the glutamate at the -1 position, GLYR1 C-terminal tripeptide, -SRE, does not function as a type 1 peroxisomal targeting signal, PTS1. GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
additional information
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due to the glutamate at the -1 position, GLYR1 C-terminal tripeptide, -SRE, does not function as a type 1 peroxisomal targeting signal, PTS1. GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
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). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T335D
phosphomimetic variant, exhibits reduced NADH-dependent hydroxypyruvate reductase activity while showing improved NADPH-dependent activity
additional information
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complementation of SSADH-deficient yeast with Arabidopsis thaliana GLYR1, the yeast then grows on 20 mM GABA as the sole nitrogen source and contains elevated levels of 4-hydroxybutyrate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, partially purified recombinant His6-tagged enzyme in an ammonium sulfate pellet, 6 months, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21 by PEG precipitation, nickel affinity and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
exclusive localization in the cytosol of transgenic Arabidopsis plants co-expressing GFP-GLYR1 and and Cherry-PTS1, a fusion protein consisting of the Cherry fluorescent protein linked to the PTS1 of the peroxisomal enzyme hydroxypyruvate reductase. Expression of N-terminal GFP-tagged or Myc-tagged GLYR1 in tobacco BY-2 cell cytosol. GFP- or Myc-tagged GLYR1 is competent, at least partially, for import into peroxisomes, since replacement of the C-terminal glutamate in GLYR1 with leucine, which yields a canonical PTS1 (i.e., a C-terminal small-basic-hydrophobic tripeptide motif), results in the modified fusion protein (GFPGLYR1-E to L and Myc-GLYR1-E to L) being dual localized to the cytosol and peroxisomes in BY-2 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GLYR isozyme transcript levels increase under various stresses, such as cold and heat
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoover, G.J.; Van Cauwenberghe, O.R.; Breitkreuz, K.E.; Clark, S.M.; Merrill, A.R.; Shelp, B.J.
Characteristics of an Arabidopsis glyoxylate reductase: general biochemical properties and substrate specificity for the recombinant protein, and developmental expression and implications for glyoxylate and succinic semialdehyde metabolism in planta
Can. J. Bot.
85
883-895
2007
Arabidopsis thaliana
Allan, W.L.; Clark, S.M.; Hoover, G.J.; Shelp, B.J.
Role of plant glyoxylate reductases during stress: a hypothesis
Biochem. J.
423
15-22
2009
Arabidopsis thaliana
Ching, S.L.; Gidda, S.K.; Rochon, A.; van Cauwenberghe, O.R.; Shelp, B.J.; Mullen, R.T.
Glyoxylate reductase isoform 1 is localized in the cytosol and not peroxisomes in plant cells
J. Integr. Plant Biol.
54
152-168
2012
Arabidopsis thaliana (Q9LSV0), Arabidopsis thaliana
Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants
Biochim. Biophys. Acta
1834
2663-2671
2013
Arabidopsis thaliana (Q9C9W5)
EXTERNAL LINKS (specific for EC-Number 1.1.1.26)
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