1.1.1.79: glyoxylate reductase (NADP+)
This is an abbreviated version!
For detailed information about glyoxylate reductase (NADP+), go to the full flat file.
Reaction
Synonyms
aac4036, At3g25530, AtGLYR1, AtGLYR2, AtGR1, AtGR2, D-2-hydroxy-acid dehydrogenase, GhrA, glycerate dehydrogenase, glyoxylate reductase, glyoxylate reductase 1, glyoxylate reductase 2, glyoxylate reductase isoform 1, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate/succinic semialdehyde reductase, GLYR1, GLYR2, GOR1, Gor1p, GR/HPR, GR1, GR2, GRHPR, GRHRP, HPR2, HPR3, More, NAD(P)H-dependent GR, NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases, PfuGRHPR, PhoGRHPR, PtGR, PyaGRHPR, TthGR1
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KM Value
KM Value on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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0.0045
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
0.016
glyoxylate
pH 7.8, temperature not specified in the publication, recombinant truncated enzyme
0.018
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
0.0304
glyoxylate
-
isoform GR1, with NADPH as cosubstrate, at pH 7.4 and 30°C
0.033
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.034
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
0.061
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.0721
glyoxylate
-
isoform GR2, with NADPH as cosubstrate, at pH 7.4 and 30°C
0.088
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.1446
glyoxylate
-
isoform GR2, with NADH as cosubstrate, at pH 7.4 and 30°C
0.181
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.2677
glyoxylate
-
isoform GR1, with NADH as cosubstrate, at pH 7.4 and 30°C
0.5
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
1.2
glyoxylate
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
3
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
4.1
glyoxylate
pH 7.5, 50°C, recombinant enzyme, with NADPH
4.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
12.4
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
0.076
NADH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
0.0009
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.0012
NADPH
with succinic semialdehyde as substrate, pH 7.6, 30°C
0.0012
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
0.0012
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
0.0014
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
0.0014
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
0.0018
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.0018
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25°C
0.002
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
0.0022
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
0.0022
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
0.0026
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
0.0027
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
0.0033
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25°C
0.0034
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
0.004
NADPH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
0.0074
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25°C
0.0084
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C
0.0088
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25°C
0.0117
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C
0.0125
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C
0.0362
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25°C
0.0648
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
0.87
recombinant protein from Escherichia coli
0.87
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
1.133
Succinic semialdehyde
isoform GLYR1, at pH 7.5 and 25°C
6.5
Succinic semialdehyde
isoform GLYR2, at pH 7.3 and 25°C
8.96
Succinic semialdehyde
with as NADPH as cofactor, pH 7.6, 30°C
8.96
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
8.96
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25°C
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics, altered cofactor kinetics of the mutant enzyme R31L/T32K/K35D/C68R compared to the wild-type
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