Any feedback?
Information on EC 1.1.1.79 - glyoxylate reductase (NADP+) and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LSV0
for references in articles please use BRENDA:EC1.1.1.79Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.79 glyoxylate reductase (NADP+)IUBMB Comments
Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
Specify your search results
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
=
+
+
+
=
+
+
Synonyms
atgr1, atglyr1, d-2-hydroxy-acid dehydrogenase, glyoxylate reductase (nadp+), atgr2, glyoxylate reductase 1, atglyr2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GLYR1
AtGR2
GLYR2
GR2
additional information
additional information
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency
additional information
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency
additional information
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycolate + NADP+ = glyoxylate + NADPH + H+
ordered Bi Bi mechanism, complexation of NADPH to the enzyme before glyoxylate or succinic semialdehyde, and release of NADP+ before glycolate or 4-hydroxybutyrate
glycolate + NADP+ = glyoxylate + NADPH + H+
the enzyme performs an acid/base catalytic mechanism involving Lys170 as the general acid and a conserved active-site water molecule
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
glycolate:NADP+ oxidoreductase
Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
CAS REGISTRY NUMBER
COMMENTARY
37250-17-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glyoxylate + NADH + H+
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glyoxylate + NADH
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
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+
-
-
-
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+
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
the highest catalytic efficiency is observed for 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 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
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
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxybutyrate
mixed type inhibition with succinic semialdehyde
NADP+
competitive with NADPH when glyoxylate is the fixed substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.033
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
0.034
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
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.6
Succinic semialdehyde
isoform GLYR1, 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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
93.5
4-hydroxybutyrate
mixed type inhibition with succinic semialdehyde
0.0095
NADP+
competitive with NADPH when glyoxylate is the fixed substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
6.8 - 7.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; (L.) Heynh
SwissProt
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; L. Heynh
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
-
glyoxylate reductase 2 is localized within the plastid, presumably in the stroma
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
evolution
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLYR1_ARATH
289
0
30692
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35900
x * 35900, truncated enzyme from Escherichia coli including His-tag
36287
x * 36287, calculated from the deduced amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 30700, isoform GLYR1, calculated from amino acid sequence
additional information
?
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
R31L/T32K/K35D/C68R
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
DELTA1-43
in contrast to the full length sequence yields a soluble protein when expressed in Escherichia coli
additional information
invertion of the cofactor specificity of the NADP+-dependent enzyme glyoxylate reductase by a structure-guided, semirational strategy, overview. The heuristic-based approach leverages the diversity and sensitivity of catalytically productive cofactor binding geometries to limit the problem to an experimentally tractable scale. Experimental validation of the CSR-SALAD method for switching cofactor preference to NAD while retaining catalytic activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, concentrated protein eluate from the affinity column, for months, enzyme activity is reasonably stable
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
nickel affinity column chromatography
recombinant His6-tagged truncated mutant enzyme from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
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 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 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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
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
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)
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
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)
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)
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
EXTERNAL LINKS (specific for EC-Number 1.1.1.79)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
