Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
glyoxylate + NADH + H+
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
additional information
?
-
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
preferred substrate
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
glyoxylate highly preferred over succinic semialdehyde as substrate
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
the affinity for glyoxylate is 10fold lower for isoform GLYR2 than that for isoform GLYR1
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
at least under oxygen deficient and high light conditions
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
reverse reaction less efficient than forward reaction
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
the affinity for succinic semialdehyde is 10fold lower for isoform GLYR2 than that for isoform GLYR1
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
involved in stress response, enhanced transcript levels of GR1 at salinity, drought, submergence, and heat and GR2 at cold and heat
-
-
?
additional information
?
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
-
-
?
additional information
?
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
-
-
?
additional information
?
-
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
glyoxylate + NADPH + H+
glycolate + NADP+
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
additional information
?
-
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
at least under oxygen deficient and high light conditions
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
involved in stress response, enhanced transcript levels of GR1 at salinity, drought, submergence, and heat and GR2 at cold and heat
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADH
much less effective than NADPH
NADH
-
NADH
much less effective than NADPH
NADP+
-
NADP+
the wild-type enzyme is specific for NADPH/NADP+
NADPH
-
NADPH
the wild-type enzyme is specific for NADPH/NADP+
NADPH
the highest catalytic efficiency is observed for NADPH
NADPH
-
-
NADPH
glyoxylate reductase 2 uses either NADPH or NADH as a cofactor, however, much greater activity is found with NADPH
NADPH
the highest catalytic efficiency is observed for NADPH
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
-
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
-
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
-
recombinant HPR3 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
-
the recombinant AtHPR2 prefers NADPH over NADH
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.87
Succinic semialdehyde
8.96
Succinic semialdehyde
additional information
additional information
-
0.0045
glyoxylate
recombinant protein from Escherichia coli
0.0045
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
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
0.0232
glyoxylate
isoform GLYR1, at pH 7.8 and 25°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
0.061
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.088
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.181
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
3
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
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
0.0009
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.0018
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.002
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
0.0034
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
0.0648
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
0.87
Succinic semialdehyde
recombinant protein from Escherichia coli
0.87
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
0.016
glyoxylate
pH 7.8, temperature not specified in the publication, recombinant truncated enzyme
0.0193
glyoxylate
isoform GLYR2, at pH 7.8 and 25°C
0.034
glyoxylate
with as NADPH as cofactor, pH 7.6, 30°C
0.034
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
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
with glyoxylate as substrate, pH 7.6, 30°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
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
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, altered cofactor kinetics of the mutant enzyme R31L/T32K/K35D/C68R compared to the wild-type
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10.1
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
0.0052
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.051
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
6.06
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
11
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
22
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
28.4
glyoxylate
isoform GLYR1, at pH 7.8 and 25°C
54.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
67.8
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
86.4
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
8.1
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
9.09
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
9.3
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
9.56
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
25.4
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
51.1
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
84.1
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
93.7
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
18.4
glyoxylate
isoform GLYR2, at pH 7.8 and 25°C
22.5
glyoxylate
with as NADPH as cofactor, pH 7.6, 30°C
22.5
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
10.7
NADPH
with succinic semialdehyde as substrate, pH 7.6, 30°C
10.7
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
10.7
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
12
NADPH
with glyoxylate as substrate, pH 7.6, 30°C
12
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
12
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
17
Succinic semialdehyde
with as NADPH as cofactor, pH 7.6, 30°C
17
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
17
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11.6
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
906
glyoxylate
isoform GLYR2, at pH 7.8 and 25°C
1.9
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25°C
0.19
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.86
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.87
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
7.45
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
14.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
72.8
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
480
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
1259
glyoxylate
isoform GLYR1, at pH 7.8 and 25°C
2870
glyoxylate
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
779
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
2870
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
3500
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
4340
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
10400
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
10900
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
24450
NADPH
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a microplate reader
51700
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
660
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
9180
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
evolution
the enzyme belongs to the group of enzymes with the most common NAD(P)-binding fold, the Rossmann fold, as well as other, less common cofactor binding folds (TIM barrel and dihydroquinoate synthase-like folds)
evolution
the primary sequence of cytosolic AtGLYR1 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR1 and beta-HAD family members, overview. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
evolution
the primary sequence of plastidial AtGLYR2 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR2 and beta-HAD family members, overview. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
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
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
-
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 30700, isoform GLYR1, calculated from amino acid sequence
?
x * 35900, truncated enzyme from Escherichia coli including His-tag
?
x * 36287, calculated from the deduced amino acid sequence
?
x * 33200, isoform GLYR2, calculated from amino acid sequence
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
-
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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
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 BL21(DE3) cells
gene GLYR1, sequence comparisons of GLYR genes and HPR genes
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
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hoover, G.J.; Prentice, G.A.; Merrill, A.R.; Shelp, B.J.
Kinetic mechanism of a recombinant Arabidopsis glyoxylate reductase: studies of initial velocity, dead-end inhibition and product inhibition
Can. J. Bot.
85
896-902
2007
Arabidopsis thaliana (Q9LSV0)
brenda
Simpson, J.P.; Di Leo, R.; Dhanoa, P.K.; Allan, W.L.; Makhmoudova, A.; Clark, S.M.; Hoover, G.J.; Mullen, R.T.; Shelp, B.J.
Identification and characterization of a plastid-localized Arabidopsis glyoxylate reductase isoform: comparison with a cytosolic isoform and implications for cellular redox homeostasis and aldehyde detoxification
J. Exp. Bot.
59
2545-2554
2008
Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9LSV0), Arabidopsis thaliana
brenda
Allan, W.L.; Simpson, J.P.; Clark, S.M.; Shelp, B.J.
Gamma-hydroxybutyrate accumulation in Arabidopsis and tobacco plants is a general response to abiotic stress: putative regulation by redox balance and glyoxylate reductase isoforms
J. Exp. Bot.
59
2555-2564
2008
Arabidopsis thaliana, Nicotiana tabacum
brenda
Allan, W.L.; Clark, S.M.; Hoover, G.J.; Shelp, B.J.
Role of plant glyoxylate reductases during stress: a hypothesis
Biochem. J.
423
15-22
2009
Arabidopsis thaliana
brenda
Ching, S.L.; Gidda, S.K.; Rochon, A.; van Cauwenberghe, O.R.; Shelp, B.J.; Mullen, R.T.
Glyoxylate reductase isoform 1 is localized in the cytosol and not peroxisomes in plant cells
J. Integr. Plant Biol.
54
152-168
2012
Arabidopsis thaliana (Q9LSV0)
brenda
Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants
Biochim. Biophys. Acta
1834
2663-2671
2013
Arabidopsis thaliana (A0A178WMD4), Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LSV0), Arabidopsis thaliana
brenda
Cahn, J.K.; Werlang, C.A.; Baumschlager, A.; Brinkmann-Chen, S.; Mayo, S.L.; Arnold, F.H.
A general tool for engineering the NAD/NADP cofactor preference of oxidoreductases
ACS Synth. Biol.
6
326-333
2016
Arabidopsis thaliana (Q9LSV0)
brenda
Cahn, J.K.; Werlang, C.A.; Baumschlager, A.; Brinkmann-Chen, S.; Mayo, S.L.; Arnold, F.H.
A general tool for engineering the NAD/NADP cofactor preference of oxidoreductases
ACS Synth. Biol.
6
326-333
2017
Arabidopsis thaliana (Q9LSV0)
brenda
Zarei, A.; Brikis, C.J.; Bajwa, V.S.; Chiu, G.Z.; Simpson, J.P.; DeEll, J.R.; Bozzo, G.G.; Shelp, B.J.
Plant glyoxylate/succinic semialdehyde reductases comparative biochemical properties, function during chilling stress, and subcellular localization
Front. Plant Sci.
8
1399
2017
Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9LSV0), Malus domestica (A0A1C8M582), Malus domestica (A0A1C8M593), Oryza sativa
brenda