Information on EC 1.1.1.26 - glyoxylate reductase

New: Word Map on EC 1.1.1.26
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
1.1.1.26
-
RECOMMENDED NAME
GeneOntology No.
glyoxylate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycolate + NAD+ = glyoxylate + NADH + H+
show the reaction diagram
can convert L-lactate
-
glycolate + NAD+ = glyoxylate + NADH + H+
show the reaction diagram
reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
-
-
Microbial metabolism in diverse environments
-
-
xylose degradation IV
-
-
SYSTEMATIC NAME
IUBMB Comments
glycolate:NAD+ oxidoreductase
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycolate oxidase
-
-
-
-
glyoxylic acid reductase
-
-
-
-
NADH-dependent glyoxylate reductase
-
-
-
-
NADH-glyoxylate reductase
-
-
-
-
reductase, glyoxylate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-32-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NADPH-dependent cytosolic termed GLYR1, and plastidial termed GLYR2 isoforms of succinic semialdehyde/glyoxylate reductase
-
-
Manually annotated by BRENDA team
non-photosynthetic mutant
-
-
Manually annotated by BRENDA team
patients with primary hyperoxaluria type 2
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
strain 12-A
-
-
Manually annotated by BRENDA team
strain CFN42, gene gxrA
-
-
Manually annotated by BRENDA team
Rhizobium etli CFN42
strain CFN42, gene gxrA
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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
physiological function
Q9LSV0
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
metabolism
-
the enzyme is involved in the glycolate metabolism, as well as the 4-hydroxybutyrate production and the GABA shunt pathway, overview
additional information
Q9LSV0
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
r
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
-
-
-
-
r
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
-
-
-
-
r
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
Q9LSV0
-
-
-
r
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
Q9C4M5
-
-
-
?
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
-
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
equilibrium is very far in direction of glycolate formation
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
GxrA
-
-
ir
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
a E141N/Q313E mutant formate dehydrogenase shows glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, overview
-
-
?
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
Rhizobium etli CFN42
-
GxrA
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
show the reaction diagram
Q97U35
-
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
show the reaction diagram
Q9C4M5
NADPH exhibits 7.5% of the activity compared to NADH
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
show the reaction diagram
-
NADPH exhibits 7.5% of the activity compared to NADH
-
-
?
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
-
preferred substrate
-
-
ir
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
located exclusively in the peroxisomes, prefers NAD+/NADH
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
Rhizobium etli, Rhizobium etli CFN42
-
GxrA
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
Q9C4M5
the relative activity for hydroxypyruvate is one-quarter that of glyoxylate in the presence of NADH as an electron donor
-
-
?
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
Rhizobium etli, Rhizobium etli CFN42
-
GxrA
-
-
ir
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
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
-
the relative activity for hydroxypyruvate is one-quarter that of glyoxylate in the presence of NADH as an electron donor
-
-
?
additional information
?
-
-
no activity with: pyruvate, 2-oxobutyrate, acetaldehyde, oxaloacetate, 2-oxoglutarate
-
-
-
additional information
?
-
-
in the endosymbiont, a 3-phosphoglycerate dehydrogenase exhibits glyoxylate/hydroxypyruvate reductase activity, substrate specificity, overview, no activity of GxrA with 2-oxoglutarate, 2-oxo-D-gluconate, and indole in the reductive direction, as well as with glycolate, D-phenyllactate, and D-gluconate in the oxidative direction
-
-
-
additional information
?
-
-
the enzyme prefers succinic semialdehyde 100fold to formaldehyde, acetaldehyde, butyraldehyde, 2-carboxybenzaldehyde, glyoxal, methylglyoxal, phenylglyoxal, and phenylglyoxylate
-
-
-
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
?
-
Rhizobium etli CFN42
-
in the endosymbiont, a 3-phosphoglycerate dehydrogenase exhibits glyoxylate/hydroxypyruvate reductase activity, substrate specificity, overview, no activity of GxrA with 2-oxoglutarate, 2-oxo-D-gluconate, and indole in the reductive direction, as well as with glycolate, D-phenyllactate, and D-gluconate in the oxidative direction
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
-
-
-
-
r
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
-
-
-
-
r
glycolate + NAD+
glyoxylate + NADH
show the reaction diagram
-
-
-
-
r
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
Q9LSV0
-
-
-
r
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
Q9C4M5
-
-
-
?
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
-
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
Rhizobium etli, Rhizobium etli CFN42
-
GxrA
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
-
-
-
-
ir
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
r
phenylpyruvate + NADH
phenyllactate + NAD+
show the reaction diagram
Rhizobium etli, Rhizobium etli CFN42
-
GxrA
-
-
ir
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
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
located exclusively in the peroxisomes, prefers NAD+/NADH
-
-
r
additional information
?
-
-
in the endosymbiont, a 3-phosphoglycerate dehydrogenase exhibits glyoxylate/hydroxypyruvate reductase activity, substrate specificity, overview
-
-
-
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
?
-
Rhizobium etli CFN42
-
in the endosymbiont, a 3-phosphoglycerate dehydrogenase exhibits glyoxylate/hydroxypyruvate reductase activity, substrate specificity, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
NAD+
-
enzyme of peroxisomes and chloroplasts prefer NAD+, enzymes of the cytosol prefer NADP+
NAD+
-
can also utilize NADP+ or O2 (reduction to H2O2) as cofactors
NADH
-
-
NADH
-
enzyme of peroxisomes and chloroplasts prefer NADH, enzymes of the cytosol prefer NADPH
NADH
-
can also utilize NADPH or O2 (reduction to H2O2) as cofactors
NADH
-
is not replacable by NADPH with GxrA
NADH
Q9C4M5
NADPH exhibits rather low activity as an electron donor compared with NADH
additional information
-
NADPH cannot replace NADH
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
Q9C4M5
1 mM, 95% inhibition
Acetohydroxamate
-
inhibits only the cytosolic enzyme type with preference for glyoxylate as substrate
Acetohydroxamate
-
inhibits only the cytosolic enzyme type with preference for glyoxylate as substrate
CuCl2
Q9C4M5
1 mM, 66% inhibition
dithiothreitol
Q9C4M5
1 mM, 50% inhibition
HgCl2
Q9C4M5
1 mM, complete inhibition
oxalate
-
inhibits only the cytosolic enzyme type with preference for hydroxypyruvate as substrate
oxalate
-
inhibits only the cytosolic enzyme type with preference for hydroxypyruvate as substrate
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
phenylhydrazine
-
-
Semicarbazide
-
-
Tartronate
-
inhibits only the cytosolic enzyme type with preference for hydroxypyruvate as substrate
Tartronate
-
inhibits only the cytosolic enzyme type with preference for hydroxypyruvate as substrate
MOPS buffer
-
50 mM at acidic and alkaline pH
additional information
Q9C4M5
a significant effect on the activity is not observed with 1 mM EDTA, 1 mM iodoacetate and 1 mM 2-mercaptoethanol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
40
2-oxobutyrate
-
pH 7.0, 37C
0.0045
glyoxylate
-
pH 7.8, 22C, recombinant His6-tagged enzyme
0.07 - 0.11
glyoxylate
-
NADPH, cytosolic enzyme
0.73
glyoxylate
Q9C4M5
pH 6.5, 50C
1.1
glyoxylate
-
NADPH, cytosolic enzyme type with preference for hydroxypyruvate as substrate
1.25
glyoxylate
-
NADPH
2.5
glyoxylate
-
pH 7.0, 37C
5
glyoxylate
Q97U35
pH 7.5, 70C, recombinant enzyme and native enzyme from xylose-grown cell extract
7.4
glyoxylate
-
pH 7.0, 30C, recombinant E141N/Q313E mutant formate dehydrogenase
10 - 25
glyoxylate
-
NADH, peroxisomal enzyme type with preference for hydroxypyruvate and NADH as substrates
0.07 - 0.12
Hydroxypyruvate
-
NADH, peroxisomal enzyme type with preference for hydroxypyruvate and NADH as substrates
0.8
Hydroxypyruvate
-
NADPH, cytosolic enzyme type with preference for hydroxypyruvate and NADPH as substrates
1.3
Hydroxypyruvate
Q9C4M5
pH 6.5, 50C
0.067
NADH
Q9C4M5
pH 6.5, 50C
0.1
NADH
Q97U35
pH 7.5, 70C, recombinant enzyme and native enzyme from xylose-grown cell extract
0.0026
NADPH
-
pH 7.8, 22C, recombinant His6-tagged enzyme
0.8
phenylpyruvate
-
pH 7.0, 37C
6.8
Hydroxypyruvate
-
pH 7.0, 37C
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
2-oxobutyrate
-
pH 7.0, 37C
1.35
glyoxylate
-
pH 7.0, 37C
2.3
glyoxylate
-
pH 7.0, 30C, recombinant E141N/Q313E mutant formate dehydrogenase
13
glyoxylate
-
pH 7.8, 22C, recombinant His6-tagged enzyme
0.25
Hydroxypyruvate
-
pH 7.0, 37C
8.1
NADPH
-
pH 7.8, 22C, recombinant His6-tagged enzyme
0.37
phenylpyruvate
-
pH 7.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.032
-
0.5 mM NADPH
0.044
-
75 mM NADH
0.05 - 0.23
-
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
-
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
44.5
Q9C4M5
pH 6.5, 50C
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 6.6
-
-
7
-
assay at, E141N/Q313E mutant formate dehydrogenase
7
-
with substrate phenylpyruvate
7.5
Q97U35
assay at
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
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
-
-
5.8 - 7.4
-
the optimal pH for hydroxypyruvate reduction is more acidic than that for glyoxylate reduction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
recombinant His6-tagged enzyme
25
-
assay at
30
-
assay at, E141N/Q313E mutant formate dehydrogenase
37
-
assay at
50
Q9C4M5
assay at
70
Q97U35
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mutant without cytosolic hydroxypyruvate-metabolizing activity
Manually annotated by BRENDA team
additional information
-
tissue-specific expression, overview
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
utilizes NADH and NADPH equally
Manually annotated by BRENDA team
-
utilizes NADH and NADPH equally
Manually annotated by BRENDA team
-
NADP+/NADPH preferring type
Manually annotated by BRENDA team
-
NADP+/NADPH preferring type
Manually annotated by BRENDA team
-
NAD+/NADH preferring type
Manually annotated by BRENDA team
-
NAD+/NADH preferring type
Manually annotated by BRENDA team
-
NAD+/NADH preferring type
Manually annotated by BRENDA team
Q9LSV0
GLYR1 is exclusively located in the cytosol
Manually annotated by BRENDA team
additional information
Q9LSV0
GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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
LITERATURE
36500 - 40000
-
calculation from DNA sequence and non-denaturing PAGE
286417
70000
-
cytosolic enzyme with preference for hydroxypyruvate as substrate
286418
76000
Q9C4M5
non-denaturimg gradient PAGE
727414
77200
-
recombinant His-tagged enzyme, gel filtration
685349
90000
-
peroxisomal enzyme with preference for hydroxypyruvate as substrate
286418
125000
-
cytosolic enzyme
286418
180000
-
thin-layer gel filtration
286408
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 33000-35000, recombinant His6-tagged enzyme, SDS-PAGE
dimer
-
2 * 38000, cytosolic enzyme with preference for hydroxypyruvate as substrate
dimer
-
2 * 41000-44000, peroxisomal enzyme with preference for hydroxypyruvate as substrate
dimer
-
2 * 37000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 38420, recombinant His-tagged enzyme, MALDI-TOF mass spectrometry
dimer
Rhizobium etli CFN42
-
2 * 37000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 38420, recombinant His-tagged enzyme, MALDI-TOF mass spectrometry
-
homodimer
Q9C4M5
2 * 37000, SDS-PAGE, 2 * 36807, calculated from sequence
homodimer
-
2 * 36807, calculated from sequence
homodimer
-
2 * 37000, SDS-PAGE, 2 * 36807, calculated from sequence
-
tetramer
-
4 * 33000, cytosolic enzyme
monomer
-
1 * 40000, SDS-PAGE
additional information
-
GLYR1 structure, molecular modelling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
Q9C4M5
10 min, stable up to
727414
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21 by PEG precipitation, nickel affinity and anion exchange chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration
-
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
Q9LSV0
expression of His6-tagged enzyme in Escherichia coli srain BL21
-
expression in Epicurean coli BL21 (DE3) as fusion protein from a His-tag plasmid
-
gene gxrA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain BL21
-
expression in Escherichia coli
Q97U35
cloned and expressed in Escherichia coli
Q9C4M5
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GLYR isozyme transcript levels increase under various stresses, such as cold and heat
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
G165D
-
mutation identified in patient with primary hyperoxaluria type 2, about 1.5% residual enzymic activity, enzyme is unstable upon purification
additional information
-
identification of point mutations and minor deletions resulting in primary hyperoxaluria type 2
R302C
-
mutation identified in patient with primary hyperoxaluria type 2, about 5.6% residual enzymic activity, enzyme is unstable upon purification
additional information
-
mutant lacking cytosolic hydroxypyruvate-metabolizing activity (HPR-1)
additional information
-
construction of a E141N/Q313E mutant formate dehydrogenase which gains glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, while the replacement induces no marked activity toward other 2-koxoacid substrates, and diminishes the enzyme's activity as to formate oxidation, substrate specificity and kinetic switch of the mutant, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
identification of point mutations and minor deletions resulting in primary hyperoxaluria type 2