Information on EC 1.1.1.26 - glyoxylate reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.26
-
RECOMMENDED NAME
GeneOntology No.
glyoxylate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycolate + NAD+ = glyoxylate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
glycolate and glyoxylate degradation
-
-
Glyoxylate and dicarboxylate metabolism
-
-
L-arabinose degradation IV
-
-
Metabolic pathways
-
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Microbial metabolism in diverse environments
-
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xylose degradation IV
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-
SYSTEMATIC NAME
IUBMB Comments
glycolate:NAD+ oxidoreductase
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-32-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
non-photosynthetic mutant
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
strain 12-A
-
-
Manually annotated by BRENDA team
parsley
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain CFN42, gene gxrA
-
-
Manually annotated by BRENDA team
strain CFN42, gene gxrA
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
maize
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme is involved in the glycolate metabolism, as well as the 4-hydroxybutyrate production and the GABA shunt pathway, overview
physiological function
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + NADH
isovalerate + NAD+
show the reaction diagram
-
GxrA
-
-
?
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
glycolate + NADP+
glyoxylate + NADPH + H+
show the reaction diagram
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
glyoxylate + NADH + H+
glycolate + NAD+
show the reaction diagram
glyoxylate + NADPH
glycolate + NADP+
show the reaction diagram
-
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
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
-
succinic semialdehyde-dependent GLYR activity potentially occurs in planta, despite the fact that glyoxylate is the preferred substrate in vitro
-
-
ir
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
glycolate + NADP+
glyoxylate + NADPH + H+
show the reaction diagram
Q9LSV0
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
-
-
-
-
ir
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
-
succinic semialdehyde-dependent GLYR activity potentially occurs in planta, despite the fact that glyoxylate is the preferred substrate in vitro
-
-
ir
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
NADPH cannot replace NADH
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
1 mM, 95% inhibition
Acetohydroxamate
CuCl2
1 mM, 66% inhibition
dithiothreitol
1 mM, 50% inhibition
HgCl2
1 mM, complete inhibition
MOPS buffer
-
50 mM at acidic and alkaline pH
oxalate
p-chloromercuribenzoate
phenylhydrazine
-
-
Semicarbazide
-
-
Tartronate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40
2-oxobutyrate
-
pH 7.0, 37C
0.0045 - 25
glyoxylate
0.07 - 6.8
Hydroxypyruvate
0.067 - 0.1
NADH
0.0026
NADPH
-
pH 7.8, 22C, recombinant His6-tagged enzyme
0.8
phenylpyruvate
-
pH 7.0, 37C
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
2-oxobutyrate
Rhizobium etli
-
pH 7.0, 37C
1.35 - 13
glyoxylate
0.25
Hydroxypyruvate
Rhizobium etli
-
pH 7.0, 37C
8.1
NADPH
Arabidopsis thaliana
-
pH 7.8, 22C, recombinant His6-tagged enzyme
0.37
phenylpyruvate
Rhizobium etli
-
pH 7.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.032
-
0.5 mM NADPH
0.044
-
75 mM NADH
0.05 - 0.23
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NADPH, cytosolic enzyme with preference for hydroxypyruvate as substrate
0.077
-
0.5 mM NADH
0.095
-
0.5 mM NADPH
0.096
-
0.5 mM NADH
0.11
-
0.5 mM NADPH
0.134
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0.5 mM NADH
0.145
-
-
0.16
-
0.5 mM NADPH
0.205
-
NADH
0.3 - 1.5
-
NADH, peroxisomal enzyme type with preference for hydroxypyruvate and NADH as substrates
0.738
-
0.5 mM NADH
7.28
-
purified recombinant His6-tagged enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 6.6
-
-
7.6
-
substrate glyoxylate
7.8
-
recombinant His6-tagged enzyme
7.9
-
Tes/K+, substrate glyoxylate
8.2
-
Tris/HCl, substrate glyoxylate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 7.8
-
pH 5.1: about 60% of activity maximum, pH 7.8: about 50% of activity maximum
5.5 - 9.5
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-
5.8 - 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
recombinant His6-tagged enzyme
25
-
assay at
30
-
assay at, E141N/Q313E mutant formate dehydrogenase
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36500 - 40000
-
calculation from DNA sequence and non-denaturing PAGE
70000
-
cytosolic enzyme with preference for hydroxypyruvate as substrate
76000
non-denaturimg gradient PAGE
77200
-
recombinant His-tagged enzyme, gel filtration
90000
-
peroxisomal enzyme with preference for hydroxypyruvate as substrate
125000
-
cytosolic enzyme
180000
-
thin-layer gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 33000-35000, recombinant His6-tagged enzyme, SDS-PAGE
homodimer
monomer
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1 * 40000, SDS-PAGE
tetramer
-
4 * 33000, cytosolic enzyme
additional information
-
GLYR1 structure, molecular modelling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
10 min, stable up to
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, partially purified recombinant His6-tagged enzyme in an ammonium sulfate pellet, 6 months, stable
-
4C, crystalline suspension in ammonium sulfate solution, 3.2 mol/l, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 by PEG precipitation, nickel affinity and anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli
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 in Epicurean coli BL21 (DE3) as fusion protein from a His-tag plasmid
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expression in Escherichia coli
expression of His6-tagged enzyme in Escherichia coli srain BL21
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gene gxrA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain BL21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GLYR isozyme transcript levels increase under various stresses, such as cold and heat
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G165D
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mutation identified in patient with primary hyperoxaluria type 2, about 1.5% residual enzymic activity, enzyme is unstable upon purification
R302C
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mutation identified in patient with primary hyperoxaluria type 2, about 5.6% residual enzymic activity, enzyme is unstable upon purification
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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identification of point mutations and minor deletions resulting in primary hyperoxaluria type 2
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