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
D-glycerate + NAD(P)+ = glyoxylate + NADPH + H+
show the reaction diagram
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-
-
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glycolate + NADP+ = glyoxylate + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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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
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Populus gelrica
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Manually annotated by BRENDA team
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UniProt
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
evolution
malfunction
metabolism
physiological function
additional information
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
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13.9% of glyoxylate activity
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?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
show the reaction diagram
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
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10.4% of glyoxylate activity
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
show the reaction diagram
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-
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
glycolate + NADP+
glyoxylate + NADPH + H+
show the reaction diagram
glyoxal + NADPH
glycol + NADP+
show the reaction diagram
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isoenzyme 1, 16% activity of glyxoxylate
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?
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
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affinity for NADPH is lower than affinity for NADH
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
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-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
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-
-
-
?
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
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?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
show the reaction diagram
NADH much less effective than NADPH
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-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
additional information
?
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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
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
show the reaction diagram
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-
-
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?
glycolate + NAD+
glyoxylate + NADH + H+
show the reaction diagram
Q9LSV0
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r
glycolate + NADP+
glyoxylate + NADPH + H+
show the reaction diagram
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
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-
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADP+
additional information
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
4-hydroxybutyrate
mixed type inhibition with NADPH; mixed type inhibition with succinic semialdehyde
adenine
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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
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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
0.0009 - 0.0648
NADPH
0.87 - 8.96
Succinic semialdehyde
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052 - 760000
glyoxylate
38 - 65
Hydroxypyruvate
4.1 - 220000
NADH
1.8 - 300000
NADPH
17
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C; with as NADPH as cofactor, pH 7.6, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 3407
glyoxylate
779 - 51700
NADPH
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
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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
24.2
purified recombinant enzyme, pH 7.5, 50°C, with NADH
61.7
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isoenzyme 2
70.1
purified recombinant enzyme, pH 7.5, 50°C, with NADPH
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
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
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.33
sequence calculation
8.5
calculated from amino acid sequence
8.54
calculated from the deduced amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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enzyme GRHPR is lost in hepatocellular carcinoma (HCC) and proliferative HCC cells
Manually annotated by BRENDA team
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; cultured with tumor necrosis factor alpha
Manually annotated by BRENDA team
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GRHPR is reduced in proliferative Huh7 cells
Manually annotated by BRENDA team
Populus gelrica
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-
Manually annotated by BRENDA team
additional information
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immunohistochemic tissue expression analysis of GRHPR, overview. GRHPR shows a lower expression in tumor tissues than in nontumoral tissues. GRHPR is negatively correlated with Ki-67
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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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)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
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
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isoenzyme 1, gel filtration
33000
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4 * 33000, SDS-PAGE
35900
x * 35900, truncated enzyme from Escherichia coli including His-tag
36200
calculated from amino acid sequence
36287
x * 36287, calculated from the deduced amino acid sequence
38000
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x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
76500
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analytical ultracentrifugation
78000
recombinant enzyme, gel filtration
82000
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gel filtration
110000
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gel filtration
125000
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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
homodimer
2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme
tetramer
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4 * 33000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure
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, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 Å 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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purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 1.75 A resolution
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
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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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purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
recombinant enzyme, 30°C, 1 h, more than 80% of activity is retained
740392
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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complete loss of activity within 10 min when incubates above 80°C
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
-
25%, unstable
n-octane
-
25%, unstable
p-xylene
-
25%, unstable
toluene
-
25%, unstable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, concentrated enzyme, can be stored for month
-80°C, concentrated protein eluate from the affinity column, for months, enzyme activity is reasonably stable
4°C, alkaline pH, no loss of activity after 1 week, at pH 7-11, 20% loss of activity
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4°C, concentrated protein eluate from the affinity column, for hours, enzyme activity is reasonably stable
4°C, diluted enzyme, storage during assays, activity starts to decrease within 30 min
isoenzyme 1, 4°C, 10 mM potassium phosphate, pH 7.0, 1 week, 20% loss of activity
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isoenzyme 2, 4°C, 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 His-tagged enzyme 2.7fold from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His6-tagged truncated mutant enzyme from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography; recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
recombinant protein from Escherichia coli
recombinant protein from Escherichia coli using His-tag
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recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, 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
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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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gene GLYR1, sequence comparisons of GLYR genes and HPR genes; gene GLYR1, sequence comparisons of GLYR genes and HPR genes, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS; gene GLYR2, sequence comparisons of GLYR genes and HPR genes, recombinant expression of a His6-tagged truncated AtGLYR2 cDNA sequence, lacking the N-terminal 58 amino acids, in Escherichia coli strain BL21 pLysS
gene PtGR, DNa and mino acid seuence determination and analysis, sequence comparisons, recombinant expresssion of His-tagged enzyme in Escherichia coli strain BL21
ORF YNL274c, DNA and amino acid sequence determination and analysis, expression in yeast strains, overview
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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) by trinitrobenzenesulphonic acid, which induces experimental colitis and intestinal epithelial cell apoptosis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D239A
site-directed mutagenesis
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
F231A
site-directed mutagenesis
K170A
site-directed mutagenesis, catalytically inactive mutant
K170E
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
K170H
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
K170R
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
N174A
site-directed mutagenesis
R31L/T32K/K35D/C68R
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site-directed mutagenesis of Rosmann fold (c.2.1.6) residues leading to a switch of cofactor preference of the enzyme from NADP(H) to NAD(H), altered cofactor kinetics of the mutant enzyme R31L/T32K/ K35D/C68R compared to the wild-type, overview
S121A
site-directed mutagenesis
T95A
site-directed mutagenesis
G160R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
enzyme glyoxylate reductase/hydroxypyruvate reductase is a prognostic marker for hepatocellular carcinoma patients after curative resection. Patients with negative GRHPR both in tumor tissues and nontumoral tissues have a significantly shorter survival time than those with positive GRHPR. Multivariate analysis establishes that GRHPR is detected in nontumoral tissues as an independent prognostic factor for patients with hepatocellular carcinoma, overview
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