Information on EC 1.1.1.79 - glyoxylate reductase (NADP+)

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

EC NUMBER
COMMENTARY hide
1.1.1.79
-
RECOMMENDED NAME
GeneOntology No.
glyoxylate reductase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycolate + NADP+ = glyoxylate + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycolate and glyoxylate degradation
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Pyruvate metabolism
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
glycolate:NADP+ oxidoreductase
Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-17-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
Populus gelrica
-
-
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Manually annotated by BRENDA team
strain BY4742, ORF YNL274c
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Manually annotated by BRENDA team
strain HB27
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-
Manually annotated by BRENDA team
NBRC code 101085
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
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-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
show the reaction diagram
-
13.9% of glyoxylate activity
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
show the reaction diagram
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
-
10.4% of glyoxylate activity
-
?
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
show the reaction diagram
-
-
-
r
glyoxal + NADPH
glycol + NADP+
show the reaction diagram
-
isoenzyme 1, 16% activity of glyxoxylate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
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
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
hydroxypyruvate + NAD(P)H
glycerate + NAD(P)+
show the reaction diagram
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
affinity for NADPH is lower than affinity for NADH
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
oxaloacetate + NADPH
malate + NADP+
show the reaction diagram
phenylpyruvate + NAD(P)H
phenyllactate + NAD(P)+
show the reaction diagram
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isoenzyme 2, 6% activity of glyoxylate
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
show the reaction diagram
NADH much less effective than NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
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 + H+
show the reaction diagram
Q9LSV0
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
show the reaction diagram
Q9LSV0
-
-
-
r
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
glyoxylate + NADPH
glycolate + NADP+
show the reaction diagram
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
4-hydroxybutyrate
mixed type inhibition with NADPH; mixed type inhibition with succinic semialdehyde
adenine
-
0.01 mM, 70% inhibition after preincubation for 5 min
alpha-ketoglutarate
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5 mM, 57% inhibition
Carbonate
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20 mM, 7-16% inhibition
chloride
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20 mM, 7-16% inhibition
cyanide
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2 mM, 46% inhibition, 20 mM, 92% inhibition
cysteine
-
isoenzyme 1, 1 mM, 29% inhibition
D-glycerate
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the enzyme shows product inhibition
diethyldicarbonate
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1 mM, 33% inhibition, incubation for 1 min
dithiothreitol
glutathione
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isoenzyme 1, 1 mM, 12% inhibition
glycidate
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10 mM, 35% inhibition after 15 min
glycolate
iodoacetamide
iodoacetate
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isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
N-ethylmaleimide
NaCl
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complete inhibition at 0.5 M
NADP+
nitrate
nitrite
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20 mM, 7-16% inhibition
p-chloromercuribenzoate
PMSF
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1 mM, 30% inhibition, incubation for 1 min
pyruvate
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5 mM, 33% inhibition
Sodium fluoride
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isoenzyme 1, 10 mM, 32% inhibition
sodium iodide
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isoenzyme 1, 50 mM, 37% inhibition of glyoxylate reduction
Sodium phosphate
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50% inhibition at 900 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
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20 mM, 17% activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045 - 16
glyoxylate
0.058 - 1.4
Hydroxypyruvate
0.013 - 2.42
NADH
0.0012 - 0.04
NADPH
0.87 - 8.96
Succinic semialdehyde
additional information
additional information
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kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.5 - 760000
glyoxylate
38 - 65
Hydroxypyruvate
4.1 - 220000
NADH
1.8 - 300000
NADPH
17
Succinic semialdehyde
Arabidopsis thaliana
F4I907, Q9LSV0
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30C; with as NADPH as cofactor, pH 7.6, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
79.9 - 93.5
4-hydroxybutyrate
22.1 - 23.7
glycolate
0.0031 - 0.147
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
-
strain BY4742, substrate glyoxylate
0.45 - 0.7
2.03
Populus gelrica
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-
3.89
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isoenzyme 1
13.8
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purified recombinant enzyme, substrate glyoxylate
61.7
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isoenzyme 2
108.1
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isoenzyme 2
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.2
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isoenzyme 1
6
Populus gelrica
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sharp optimum, 55% and 23% activity at pH 7.0 and 8.0 respectively
6 - 7.5
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reduction of hydroxypyruvate
6.2
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reduction of hydroxypyruvate
6.45
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enzyme activity decreases by 40% and 50% at pH 5.5 and 8.0 respectively
6.5 - 7.4
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-
6.8 - 7.8
; with glyoxylate and NADPH
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
Populus gelrica
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23% of maximal activity at pH 8.0
5.5 - 9
approximately 10% of activity at pH 5.5 and 9
6.7
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recombinant protein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
calculated from amino acid sequence
8.54
calculated from the deduced amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Populus gelrica
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-
Manually annotated by BRENDA team
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
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus yayanosii (strain CH1 / JCM 16557)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
isoenzyme 1, gel filtration
36200
calculated from amino acid sequence
76500
-
analytical ultracentrifugation
82000
-
gel filtration
110000
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gel filtration
125000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35900, truncated enzyme from Escherichia coli including His-tag; x * 36287, calculated from the deduced amino acid sequence
tetramer
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4 * 33000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
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sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
60% loss of activity after 10 min, activity is completely lost above 60C
80
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complete loss of activity within 10 min when incubates above 80C
82
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melting point
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,5-pentanediol
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25%, half life reduced by approximately 70%
diethylene glycol
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half-life in the presence of 25% diethylene glycol significantly longer than that in the absence of an organic solvent
dimethyl sulfoxide
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half-life in the presence of 25% dimethyl sulfoxide significantly longer than that in the absence of an organic solvent
Ethanol
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25%, half life reduced by approximately 70%
Glycerol
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25%, unstable
n-decane
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25%, unstable
n-hexane
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25%, unstable
n-octane
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25%, unstable
p-xylene
-
25%, unstable
toluene
-
25%, unstable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, concentrated enzyme, can be stored for month
-80C, concentrated protein eluate from the affinity column, for months, enzyme activity is reasonably stable
4C, alkaline pH, no loss of activity after 1 week, at pH 7-11, 20% loss of activity
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4C, concentrated protein eluate from the affinity column, for hours, enzyme activity is reasonably stable
4C, diluted enzyme, storage during assays, activity starts to decrease within 30 min
isoenzyme 1, 4C, 10 mM potassium phosphate, pH 7.0, 1 week, 20% loss of activity
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isoenzyme 2, 4C, 10 mM, potassium phosphate, pH 7.0, 20% glycerol, 1 week, 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, affinity chromatography, Sephadex G-75SF, AgdApP-4
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centrifugation at 10500g, isoelectric focusing
Populus gelrica
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ethanol precipitation, DEAE-cellulose, CM-cellulose, affinity chromatography
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isoenzyme 1, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, hydroxylapatite
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isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxyapatite, Sephadex G-150, phosphocellulose
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isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, phospho-cellulose
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nickel affinity column chromatography; recombinant truncated protein using His-tag
recombinant C-terminally His9-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
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recombinant enzyme; recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, the His-tag is cleaved by thrombin followed by gel filtration, over 95% purity
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recombinant protein from Escherichia coli
recombinant protein from Escherichia coli using His-tag
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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
expressed as GFP-fusion protein in tobacco BY-2 cells; expressed as GFP-fusion protein in tobacco BY-2 cells; expressed as His-tag fusion protein in E. coli BL-21(DE3) Rosetta (pLysS), full-length and truncated GR2 sequences introduced into Escherichia coli, only the recombinant truncated GR2 is soluble, expression markedly improved by co-expression of the GroES/GroEL chaperone; expressed in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells and in Nicotiana tabacum BY-2 cells
expressed in Escherichia coli
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE
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expressed in Escherichia coli Top10 as His-tag fusion protein
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expression in Escherichia coli strain JM109
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expression of His-tagged wild-type and mutant enzymes in Escherichia coli
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expression of the Myc-His9-tagged enzyme in Escherichia coli
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ORF YNL274c, DNA and amino acid sequence determination and analysis, expression in yeast strains, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1-43
in contrast to the full length sequence yields a soluble protein when expressed in Escherichia coli
DELTA2-45
localizes in the cytosol instead of plastids
G160R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
Show AA Sequence (2838 entries)
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