HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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 expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
=
+
+
+
=
+
+
Synonyms
At3g25530, AtGLYR1, AtGLYR2, AtGR1, AtGR2, D-2-hydroxy-acid dehydrogenase, glycerate dehydrogenase, glyoxylate reductase, glyoxylate reductase 1, glyoxylate reductase 2, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtGR1
AtGR2
glyoxylate reductase
glyoxylate reductase/hydroxypyruvate reductase
GLYR1
GLYR2
GOR1
GR2
GRHPR
GRHRP
NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases
PtGR
PyaGRHPR
TthGR1
-
belongs to the D-2-hydroxyacid dehydrogenase family, enzyme used NADPH and NADH (EC 1.1.1.26 activity) as cofactor
additional information
GRHPR
; bifunctional enzyme with glyoxylate reductase and hydroxypyruvate reductase activities
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
-
the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
-
enzyme shows NADH- and NADPH-dependent glyoxylate reductase (EC 1.1.1.26 or 1.1.1.79) activity with higher efficiency with NADH but higher affinity for NADPH when enzyme is incubated without substrate, enzyme displays also hydroxypyruvate reductase (EC 1.1.1.81) activity, closely related to D-glycerate dehydrogense (EC 1.1.1.29)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glycerate + NAD(P)+ = glyoxylate + NADPH + H+
-
-
-
-
glycolate + NADP+ = glyoxylate + NADPH + H+
-
-
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
glycolate:NADP+ oxidoreductase
Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37250-17-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
13.9% of glyoxylate activity
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
10.4% of glyoxylate activity
-
?
glyoxal + NADPH
glycol + NADP+
-
isoenzyme 1, 16% activity of glyxoxylate
-
?
hydroxypyruvate + NADH
D-glycerate + NAD+
-
affinity for NADPH is lower than affinity for NADH
-
-
?
phenylpyruvate + NAD(P)H
phenyllactate + NAD(P)+
-
isoenzyme 2, 6% activity of glyoxylate
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
enzyme prefers NADPH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme plays a protective role in detoxification of glyoxylate
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
isoenzyme 2, 16% activity with NADH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
7% of activity with glyoxylate
-
-
glyoxylate + NAD(P)H
glycolate + NAD(P)+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
glyoxylate + NADH
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADH
glycolate + NAD+
-
affinity for NADPH is lower than affinity for NADH
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADPH
glycolate + NADP+
-
key enzyme in glyoxylate pathway. The regulation of the GHPR expression by peroxisome proliferator-activated receptor alpha may contribute to energy homeostasis by modulating the carbon supply for gluconeogenesis
-
-
?
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+
-
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
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
preferred substrate
-
-
?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
-
25 mM hydroxypyruvate, 68% of the activity with glyoxylate, 2.5 mM hydroxypyruvate, isoenzyme 2, 332% of the activity of glyoxylate
-
?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
-
isoenzyme 1, hydroxypyruvate shows 15% of the activity of glyoxylate
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
15% activity compared to glyoxylate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
15% activity compared to glyoxylate
-
-
?
oxaloacetate + NADPH
malate + NADP+
-
28.6% of glyoxylate activity
-
?
oxaloacetate + NADPH
malate + NADP+
-
isoenzyme 1, 12% activity of glyoxylate
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
r
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
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
?
-
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 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
?
-
-
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
-
-
-
additional information
?
-
-
structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
-
-
-
additional information
?
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
-
additional information
?
-
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
-
additional information
?
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
-
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
-
substrate specificity, several 2-oxo compounds including phenylpyruvate, pyruvate, methylglyoxal, and oxaloacetate act as inert electron acceptors, as do glycolate and malate, overview
-
-
-
additional information
?
-
-
phenylpyruvate, pyruvate, methylglyoxal, malate, and oxaloacetate not suitable as substrate
-
-
-
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
substrate specificity, several 2-oxo compounds including phenylpyruvate, pyruvate, methylglyoxal, and oxaloacetate act as inert electron acceptors, as do glycolate and malate, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
glycolate + NADP+
glyoxylate + NADPH + H+
A0A178WMD4, F4I907, Q9CA90
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
A0A0H3U0Y7
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
enzyme prefers NADPH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme plays a protective role in detoxification of glyoxylate
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
glyoxylate + NADPH
glycolate + NADP+
-
key enzyme in glyoxylate pathway. The regulation of the GHPR expression by peroxisome proliferator-activated receptor alpha may contribute to energy homeostasis by modulating the carbon supply for gluconeogenesis
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
F4I907, Q9LSV0
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+
F4I907, Q9LSV0
detoxification of succinic semialdehyde during stress
-
-
r
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
?
-
A0A178WMD4
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
?
-
F4I907
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
Q9CA90
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
A0A178WMD4
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
?
-
F4I907
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
?
-
Q9CA90
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
?
-
A0A178WMD4
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
?
-
F4I907
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
?
-
Q9CA90
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
?
-
A0A178WMD4
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
?
-
F4I907
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
-
additional information
?
-
Q9CA90
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
-
additional information
?
-
-
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
-
-
-
additional information
?
-
Q8U3Y2
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
F8AEA4
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
additional information
?
-
F8AEA4
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADH
much less effective than NADPH; much less effective than NADPH
NADPH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
-
preferred cofactor, yields lower Km but similar turnover than NADH
NADPH
glyoxylate reductase 2 uses either NADPH or NADH as a cofactor, however, much greater activity is found with NADPH
NADPH
-
preferred cofactor, NADH gives only 4% of the activity with NADPH
additional information
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
-
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
-
additional information
-
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
-
additional information
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
-
additional information
the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview
-
additional information
-
the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxybutyrate
mixed type inhibition with NADPH; mixed type inhibition with succinic semialdehyde
iodoacetate
-
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
sodium iodide
-
isoenzyme 1, 50 mM, 37% inhibition of glyoxylate reduction
dithiothreitol
-
isoenzyme 1, 1 mM, 41% inhibition, 10 mM, 87% inhibition
glycolate
mixed type inhibition with glyoxylate; uncompetitive with NADPH
iodoacetamide
-
isoenzyme 2, 1 mM, 87% inhibition, isoenzyme 1, 1 mM, 17% inhibition
NADP+
competitive with NADPH; competitive with NADPH when glyoxylate is the fixed substrate; uncompetitive with glyoxylate; uncompetitive with succinic semialdehyde
p-chloromercuribenzoate
-
0.1 mM, 55% inhibition after preincubation for 5 min
p-chloromercuribenzoate
-
isoenzyme 2, 1 mM, complete inhibition, 0.1 mM, 88% inhibition, 29% inhibition in the presence of 1 mM dithiothreitol, 21% inhibition in the presence of 1 mM L-cysteine, isoenzyme 1, 1 mM, 59% inhibition
additional information
-
no activity at more than 500 mM NaCl, 50% activity in the presence of 900 mM sodium phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperoxaluria, Primary
Up regulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis.
Liver Cirrhosis
Association between angiotensin II type 1 receptor polymorphisms and the occurrence of nonalcoholic fatty liver disease.
Neoplasms
Identification of NPAC as a novel biomarker and regulator for hepatocellular carcinoma.
Non-alcoholic Fatty Liver Disease
Association between angiotensin II type 1 receptor polymorphisms and the occurrence of nonalcoholic fatty liver disease.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.016
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
0.033
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; with as NADPH as cofactor, pH 7.6, 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
0.088
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
0.24
glyoxylate
-
37°C, cofactor: NADPH; pH 7.5, 37°C, recombinant enzyme, with NADPH
0.5
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
1
glyoxylate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
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
0.058
Hydroxypyruvate
-
37°C, cofactor: NAPDH; pH 7.5, 37°C, recombinant enzyme, with NADPH
0.19
Hydroxypyruvate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
0.076
NADH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
0.0009
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.0012
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C; with succinic semialdehyde 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; with glyoxylate as substrate, pH 7.6, 30°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
0.002
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
0.0027
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
0.004
NADPH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant 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
8.96
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C; with as NADPH as cofactor, pH 7.6, 30°C
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C; with as NADPH as cofactor, pH 7.6, 30°C
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
22.5
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C; with as NADPH as cofactor, pH 7.6, 30°C
27
glyoxylate
-
37°C, cofactor: NADPH; pH 7.5, 37°C, recombinant enzyme, with NADPH
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
glyoxylate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
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 enyzme
65000
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
76000
glyoxylate
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
38
Hydroxypyruvate
-
37°C, cofactor: NAPDH; pH 7.5, 37°C, recombinant enzyme, with NADPH
65
Hydroxypyruvate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
22000
NADH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
9.09
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
9.56
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
10.7
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C; with succinic semialdehyde 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; with glyoxylate as substrate, pH 7.6, 30°C
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
30000
NADPH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 enyzme
779
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.45 - 0.7
24.2
purified recombinant enzyme, pH 7.5, 50°C, with NADH
70.1
purified recombinant enzyme, pH 7.5, 50°C, with NADPH
additional information
additional information
-
activities of wild-type and mutant strains, overview
additional information
-
3 micromol/min mg chlorophyll, chloroplast preparations
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.45
-
enzyme activity decreases by 40% and 50% at pH 5.5 and 8.0 respectively
6.7
7.5
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia; putative uncharacterized protein At1g17650; ecotype Columbia
UniProt
brenda
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; (L.) Heynh
SwissProt
brenda
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; L. Heynh
SwissProt
brenda
L. Heynh ecotype Columbia, plants exposed to the stress factors drought, salinity, submergence, cold, or heat
-
-
brenda
L., cv. Samsun NN, plants exposed to the stress factor submergence
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme GRHPR is lost in hepatocellular carcinoma (HCC) and proliferative HCC cells
brenda
additional information
-
immunohistochemic tissue expression analysis of GRHPR, overview. GRHPR shows a lower expression in tumor tissues than in nontumoral tissues. GRHPR is negatively correlated with Ki-67
brenda
-
; the enzyme plays a critical role in the removal of the metabolic by-product glyoxylate from within the liver. Deficiency of this enzyme is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
-
brenda
glyoxylate reductase 2 is localized within the plastid, presumably in the stroma; stroma
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family; 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; 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; 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
evolution
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
evolution
-
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
evolution
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
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 deduced amino acid sequence of the enzyme from Paecilomyes thermophila has low similarities to the reported glyoxylate reductases
evolution
-
the deduced amino acid sequence of the enzyme from Paecilomyes thermophila has low similarities to the reported glyoxylate reductases
-
evolution
-
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
-
malfunction
-
enzyme deficiency is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure. Upregulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis, the phenomenon also occurs in patients with Crohn's disease. Overexpression of GRHPR is accompanied by active caspase-3 and cleaved poly ADP-ribose polymerase (PARP) accumulation. Knockdown of GRHPR inhibits the accumulation of active caspase-3 and cleaved PARP in TNF-alpha treated HT-29 cells
metabolism
-
glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a key enzyme in the glyoxylate cycle
metabolism
glyoxylate reductase is an important enzyme involved in theglyoxylate metabolism in organism
metabolism
-
glyoxylate reductase is an important enzyme involved in theglyoxylate metabolism in organism
-
physiological function
-
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
physiological function
-
human glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a D-2 hydroxy-acid dehydrogenase that plays a critical role in the removal of the metabolic by-product glyoxylate from the liver; upregulation of glyoxylate reductase/hydroxypyruvate reductase is associated with intestinal epithelial cells apoptosis in trinitrobenzenesulfonic acid-induced colitis
physiological function
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulate the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
physiological function
-
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
physiological function
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
physiological function
-
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
-
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
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
-
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
-
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
-
Show AA Sequence and Transmembrane Helices (5949 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Rhizobium meliloti (strain 1021)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35900
x * 35900, truncated enzyme from Escherichia coli including His-tag
36000
36287
x * 36287, calculated from the deduced amino acid sequence
38000
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
36000
-
2 * 36000, SDS-PAGE, native mass by gel filtration (native mass not given in the reference)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 35900, truncated enzyme from Escherichia coli including His-tag; x * 36287, calculated from the deduced amino acid sequence
dimer
homodimer
additional information
dimer
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
dimer
-
2 * 36000, SDS-PAGE, native mass by gel filtration (native mass not given in the reference)
homodimer
2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme
homodimer
-
2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme
-
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
the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
additional information
-
the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
additional information
-
the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 Å resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
-
purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 1.75 A resolution
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
-
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD
-
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-43
in contrast to the full length sequence yields a soluble protein when expressed in Escherichia coli
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
G160R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
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
additional information
constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
additional information
-
constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
additional information
constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
additional information
-
constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
-
additional information
-
deletion of the glyoxylate reductase-encoding gene leads to higher biomass concentration after diauxic shift, overview
additional information
-
deletion of the glyoxylate reductase-encoding gene leads to higher biomass concentration after diauxic shift, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
recombinant enzyme, 30°C, 1 h, more than 80% of activity is retained
740392
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
70
80
-
complete loss of activity within 10 min when incubates above 80°C
40
-
isoenzyme 2, 90% loss of activity after 5 min, 20% glycerol protects from inactivation, enzyme retains 65% of its activity after 5 min at 40°C
40
-
isoenzyme 1, 20% loss of activity after 5 min, complete inactivation above 50°C
50
-
60% loss of activity after 10 min, activity is completely lost above 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diethylene glycol
-
half-life in the presence of 25% diethylene glycol significantly longer than that in the absence of an organic solvent
dimethyl sulfoxide
-
half-life in the presence of 25% dimethyl sulfoxide significantly longer than that in the absence of an organic solvent
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, concentrated protein eluate from the affinity column, for months, enzyme activity is reasonably stable
4°C, alkaline pH, no loss of activity after 1 week, at pH 7-11, 20% loss of activity
-
4°C, concentrated protein eluate from the affinity column, for hours, enzyme activity is reasonably stable
4°C, diluted enzyme, storage during assays, activity starts to decrease within 30 min
isoenzyme 1, 4°C, 10 mM potassium phosphate, pH 7.0, 1 week, 20% loss of activity
-
isoenzyme 2, 4°C, 10 mM, potassium phosphate, pH 7.0, 20% glycerol, 1 week, 10% loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ethanol precipitation, DEAE-cellulose, CM-cellulose, affinity chromatography
-
isoenzyme 1, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, hydroxylapatite
-
isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxyapatite, Sephadex G-150, phosphocellulose
-
isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, phospho-cellulose
-
nickel affinity column chromatography; recombinant truncated protein using His-tag
recombinant C-terminally His9-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
-
recombinant enzyme; recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, the His-tag is cleaved by thrombin followed by gel filtration, over 95% purity
-
recombinant His-tagged enzyme 2.7fold from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His6-tagged truncated mutant enzyme from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography; recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
recombinant protein from Escherichia coli
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
exclusive localization in the cytosol of transgenic Arabidopsis plants co-expressing GFP-GLYR1 and and Cherry-PTS1, a fusion protein consisting of the Cherry fluorescent protein linked to the PTS1 of the peroxisomal enzyme hydroxypyruvate reductase. Expression of N-terminal GFP-tagged or Myc-tagged GLYR1 in tobacco BY-2 cell cytosol. GFP- or Myc-tagged GLYR1 is competent, at least partially, for import into peroxisomes, since replacement of the C-terminal glutamate in GLYR1 with leucine, which yields a canonical PTS1 (i.e., a C-terminal small-basic-hydrophobic tripeptide motif), results in the modified fusion protein (GFPGLYR1-E to L and Myc-GLYR1-E to L) being dual localized to the cytosol and peroxisomes in BY-2 cells
-
expressed as GFP-fusion protein in tobacco BY-2 cells; expressed as GFP-fusion protein in tobacco BY-2 cells; expressed as His-tag fusion protein in E. coli BL-21(DE3) Rosetta (pLysS), full-length and truncated GR2 sequences introduced into Escherichia coli, only the recombinant truncated GR2 is soluble, expression markedly improved by co-expression of the GroES/GroEL chaperone; expressed in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells and in Nicotiana tabacum BY-2 cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE
-
gene GLYR1, sequence comparisons of GLYR genes and HPR genes; gene GLYR1, sequence comparisons of GLYR genes and HPR genes, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS; gene GLYR2, sequence comparisons of GLYR genes and HPR genes, recombinant expression of a His6-tagged truncated AtGLYR2 cDNA sequence, lacking the N-terminal 58 amino acids, in Escherichia coli strain BL21 pLysS
gene PtGR, DNa and mino acid seuence determination and analysis, sequence comparisons, recombinant expresssion of His-tagged enzyme in Escherichia coli strain BL21
ORF YNL274c, DNA and amino acid sequence determination and analysis, expression in yeast strains, overview
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) by trinitrobenzenesulphonic acid, which induces experimental colitis and intestinal epithelial cell apoptosis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
enzyme glyoxylate reductase/hydroxypyruvate reductase is a prognostic marker for hepatocellular carcinoma patients after curative resection. Patients with negative GRHPR both in tumor tissues and nontumoral tissues have a significantly shorter survival time than those with positive GRHPR. Multivariate analysis establishes that GRHPR is detected in nontumoral tissues as an independent prognostic factor for patients with hepatocellular carcinoma, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yokota, A.; Kitaoka, S.
Occurrence and subcellular distribution of enzymes involved in the glycolate pathways and their physiological function in a bleached mutant of Euglena gracilis Z.
Agric. Biol. Chem.
45
15-22
1981
Euglena gracilis
-
brenda
Kleczkowski, L.A.
Kinetics and regulation of the NAD(P)H-dependent glyoxylate-specific reductase from spinach leaves
Z. Naturforsch. C
50
21-28
1995
Spinacia oleracea
-
brenda
Husic, D.W.; Tolbert, N.E.
NADH:hydroxypyruvate reductase and NADPH:glyoxylate reductase in algae: partial purification and characterization from Chlamydomonas reinhardtii
Arch. Biochem. Biophys.
252
396-408
1987
Chlamydomonas reinhardtii
brenda
Kleczkowski, L.A.; Randall, D.D.; Blevins, D.G.
Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase
Biochem. J.
239
653-659
1986
Glycine max, Spinacia oleracea, Triticum aestivum
brenda
Yokota, A.; Haga, S.; Kitaoka, S.
Purification and some properties of glyoxylate reductase (NADP+) and its functional location in mitochondria in Euglena gracilis Z
Biochem. J.
227
211-216
1985
Euglena gracilis
brenda
Mulligan, R.M.; Wilson, B.; Tolbert, N.E.
Effects of glyoxylate on photosynthesis by intact chloroplasts
Plant Physiol.
72
415-419
1983
Spinacia oleracea
brenda
Fukuda, H.; Moriguchi, M.; Kimura, A.; Tochikura, T.
Purification and properties of glyoxylate reductase from Neurospora crassa
Agric. Biol. Chem.
45
1153-1158
1981
Neurospora crassa
-
brenda
Fukuda, H.; Moriguchi, M.; Tochikura, T.
Purification and enzymatic properties of glyoxylate reductase II from baker's yeast
J. Biochem.
87
841-846
1980
Saccharomyces cerevisiae
brenda
Sagisaka, S.
Occurrence of nicotinamide adenine dinucleotide phosphate-linked glyoxylate reductase in nonphotosynthetic xylem tissue of perennials
Plant Physiol.
65
377-381
1980
Populus gelrica
brenda
Yokota, A.; Kitaoka, S.
Occurrence and properties of the glycollate-glyoxylate shuttle in mitochondria of Euglena gracilis z
Biochem. J.
184
189-192
1979
Euglena gracilis
brenda
Tochikura, T.; Fukuda, H.; Moriguchi, M.
Purification and properties of glyoxylate reductase I from baker's yeast
J. Biochem.
86
105-110
1979
Saccharomyces cerevisiae
brenda
Zeltich, I.
Effect of glycidate, an inhibitor of glycolate synthesis in leaves, on the activity of some enzymes of the glycolate pathway
Plant Physiol.
61
236-241
1978
Nicotiana tabacum
brenda
Mdluli, K.; Booth, M.P.; Brady, R.L.; Rumsby, G.
A preliminary account of the properties of recombinant human glyoxylate reductase (GRHPR), LDHA and LDHB with glyoxylate, and their potential roles in its metabolism
Biochim. Biophys. Acta
1753
209-216
2005
Homo sapiens
brenda
Genolet, R.; Kersten, S.; Braissant, O.; Mandard, S.; Tan, N.S.; Bucher, P.; Desvergne, B.; Michalik, L.; Wahli, W.
Promoter rearrangements cause species-specific hepatic regulation of the glyoxylate reductase/hydroxypyruvate reductase gene by the peroxisome proliferator-activated receptor alpha
J. Biol. Chem.
280
24143-24152
2005
Homo sapiens, Mus musculus
brenda
Booth, M.P.; Conners, R.; Rumsby, G.; Brady, R.L.
Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase
J. Mol. Biol.
360
178-189
2006
Homo sapiens
brenda
Yoshikawa, S.; Arai, R.; Kinoshita, Y.; Uchikubo-Kamo, T.; Wakamatsu, T.; Akasaka, R.; Masui, R.; Terada, T.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate
Acta Crystallogr. Sect. D
63
357-365
2007
Pyrococcus horikoshii OT3
brenda
Ogino, H.; Nakayama, H.; China, H.; Kawata, T.; Doukyu, N.; Yasuda, M.
Characterization of recombinant glyoxylate reductase from thermophile Thermus thermophilus HB27
Biotechnol. Prog.
24
321-325
2008
Thermus thermophilus, Thermus thermophilus HB27, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
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, Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9LSV0)
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
Rintala, E.; Pitkanen, J.; Vehkomaki, M.; Penttila, M.; Ruohonen, L.
The ORF YNL274c (GOR1) codes for glyoxylate reductase in Saccharomyces cerevisiae
Yeast
24
129-136
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
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, Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LSV0)
brenda
Pan, Y.; Ni, R.; Deng, Q.; Huang, X.; Zhang, Y.; Lu, C.; Li, F.; Huang, D.; He, S.; Chen, B.
Glyoxylate reductase/hydroxypyruvate reductase: a novel prognostic marker for hepatocellular carcinoma patients after curative resection
Pathobiology
80
155-162
2013
Homo sapiens (Q9UBQ7)
brenda
Zong, C.; Nie, X.; Zhang, D.; Ji, Q.; Qin, Y.; Wang, L.; Jiang, D.; Gong, C.; Liu, Y.; Zhou, G.
Up regulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis
Pathol. Res. Pract.
212
365-371
2016
Homo sapiens, Homo sapiens (Q9UBQ7)
brenda
Lassalle, L.; Engilberge, S.; Madern, D.; Vauclare, P.; Franzetti, B.; Girard, E.
New insights into the mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductases
Sci. Rep.
6
20629
2016
Pyrococcus furiosus (Q8U3Y2), Pyrococcus horikoshii, Pyrococcus yayanosii (F8AEA4), Pyrococcus yayanosii CH1 (F8AEA4)
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
Duan, X.; Hu, S.; Zhou, P.; Zhou, Y.; Liu, Y.; Jiang, Z.
Characterization and crystal structure of a first fungal glyoxylate reductase from Paecilomyes thermophila
Enzyme Microb. Technol.
60
72-79
2014
Paecilomyces sp. 'thermophila' (A0A0H3U0Y7), Paecilomyces sp. 'thermophila', Paecilomyces sp. 'thermophila' J18 (A0A0H3U0Y7)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.79)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
