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Information on EC 1.1.1.81 - hydroxypyruvate reductase
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EC Tree
1.1.1.81 hydroxypyruvate reductaseSpecify your search results
Word Map
- 1.1.1.81
- peroxisomal
- glyoxylate
-
photorespiration
- microbodies
-
photorespiratory
- glyoxysomes
-
pumpkin
- hyphomicrobium
- extorquens
- methylobacterium
-
hexulose
- methylovorum
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
At1g12550, AtHPR1, beta-hydroxypyruvate reductase, D-2-hydroxy-acid dehydrogenase, D-glycerate dehydrogenase, glycerate dehydrogenase, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate/hydroxypyruvate reductase, GLYR1, GRHPR, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-hydroxypyruvate reductase
-
-
-
-
D-glycerate dehydrogenase
-
-
-
-
glyoxylate reductase/hydroxypyruvate reductase
glyoxylate/hydroxypyruvate reductase
GRHPR
HPR1
HPR2
HPR3
HRP
hydroxypyruvate reductase
NADH:hydroxypyruvate reductase
-
-
-
-
additional information
GRHPR
bifunctional enzyme with glyoxylate reductase and hydroxypyruvate reductase activities
additional information
-
the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
-
the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
-
hydroxypyruvate reductase (EC 1.1.1.81) activity is found for the same protein showing NADH- and NADPH-dependent glyoxylate reductase (EC 1.1.1.26 or 1.1.1.79) activity, closely related to D-glycerate dehydrogense (EC 1.1.1.29)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NADP+ 2-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9059-44-3
-
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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
2,3-butandione + NAD(P)H
butan-2-ol-3-one + NAD(P)+
-
33 mM, 12% of activity with hydroxypyruvate
-
?
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
-
33 mM, 14% of activity with hydroxypyruvate
-
?
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
-
-
-
?
oxaloacetate + NAD(P)H
malate + NAD(P)+
-
33 mM, 32% of activity with hydroxypyruvate
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
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)+
-
cofactor NADH, 15% of activity with hydroxypyruvate, cofactor NADPH, 1.5% of activity with hydroxypyruvate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
33 mM, 15% activity
-
-
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
activity with hydroxypyruvate and NADPH is 2fold higher than with other pair of reactants
-
ir
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
cofactor NADPH, 80% of activity with NADH, rate of oxidation reaction: 1.5% of reduction reaction only with cofactor NADH
-
r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
Nicotiana tabacum cv. SR1
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?, r
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
-
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
-
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
-
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
-
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
-
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 transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
-
-
-
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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
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
-
-
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
cofactor NADPH, 80% of activity with NADH, rate of oxidation reaction: 1.5% of reduction reaction only with cofactor NADH
-
r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
Nicotiana tabacum cv. SR1
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
-
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
-
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
-
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
?
-
-
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADH
isoform HPR1 prefers NADH over NADPH; isoform HPR2 prefers NADPH over NADH; isoform HPR3 prefers NADPH over NADH
NADPH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
preferred cofactor of HPR2; shows some reactivity with NADPH
NADPH
isoform HPR1 prefers NADH over NADPH; isoform HPR2 prefers NADPH over NADH; isoform HPR3 prefers NADPH over NADH
additional information
recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-diphospho-D-glycerate
-
1 mM, 83% and 91% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
2-phospho-DL-glycerate
-
1 mM, 93% and 81% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
3-phospho-D-glycerate
-
1 mM, 53% and 65% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
alpha-D-fructose 1,6-diphosphate
-
0.1 mM, 28% and 74% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
ATP
-
1 mM, 62% and 64% inhibition of liver and spinal cord enzyme respectively, 73% and 89% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
glyoxylate
-
10 mM, 55% inhibition of NADH linked hydroxypyruvate reduction, 15% of NADPH linked reduction, 80% of NAD+ linked glycerate oxidation
NAD+
-
4 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 60% of NADPH linked reduction
NADP+
-
4 mM, 15% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction, 8% of NAD+ linked glycerate oxidation
oxaloacetate
-
2.5 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 20% of NADPH linked reduction
citrate
-
5 mM, 20% inhibition of NADH linked hydroxypyruvate reduction, 25% of NADPH linked reduction
D-glycerate
-
5 mM, 20% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction
Hydroxypyruvate
-
2 mM, 79% inhibition of enzyme activity in LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
Hydroxypyruvate
-
0.5 mM, 90% of NAD+ linked glycerate oxidation
phosphohydroxypyruvate
-
0.025 mM, 66% and 64% inhibition of liver and spinal cord enzyme respectively
pyruvate
-
1 mM, 73% and 89% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
pyruvate
-
10 mM, 40% inhibition of NADH linked hydroxypyruvate reduction
Tartronate
-
2 mM, 83% inhibition of enzyme activity in LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
-
80 mM, 8fold increase in hydroxypyruvate reductase activity, reaction rate increases with an increase in NaCl concentration up to 200 mM, but diminishes if the salt concentration is greater
additional information
-
in the dark, cytokinins mimic the regulatory effect of light upon algal cell division, metabolite content and stimulate carbon recycling for Calvin cycle reactions by enhancing of light-dependent NADH-HPR activity by up to 62%, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Ethanolic dehydration and its effect on membrane-bound enzymes of Chlorogloeopsis fritschii and Chlorella pyrenoidosa.
Hyperoxaluria, Primary
Identification of missense, nonsense, and deletion mutations in the GRHPR gene in patients with primary hyperoxaluria type II (PH2).
Hyperoxaluria, Primary
The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0038
Hydroxypyruvate
-
value increases with NaCl concentrations higher than 10 mM
0.08
Hydroxypyruvate
-
enzyme activity of wild-type in 40-60% precipitate fractions after ammonium sulfate fractionation
0.09
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
0.165
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
0.41
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
0.71
Hydroxypyruvate
-
enzyme activity of LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase in 40-60% precipitate fractions after ammonium sulfate fractionation
6.1
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
10
Hydroxypyruvate
-
enzyme in high-salt fraction of DEAE-cellulose chromatography
40
Hydroxypyruvate
-
enzyme in low-salt fraction of DEAE-cellulose chromatography
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.5
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.232
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0162
-
enzyme activity in crude leaf extracts of LaPr 88/29 mutant which exhibits no NADH-dependent hydroxypyruvate activity
0.054
-
enzyme activity in leaf extracts of LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
broad optimum between pH 4.0 and 6.5 for hydroxypyruvate reduction
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
; both HPR1 and HPR2 (EC 1.1.1.81) are the major hydroxypyruvate-reducing enzymes in leaves
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
about 70% of NADPH-dependent hydroxypyruvate reductase activity is localized in the cytosol, minor activities in chlorplasts and peroxisomes
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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; 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 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
physiological function
physiological function
-
in the dark, cytokinins mimic the regulatory effect of light upon algal cell division, metabolite content and stimulate carbon recycling for Calvin cycle reactions by enhancing of light-dependent NADH-HPR activity, regulation, overview
physiological function
deletion of any of the core enzymes of the photorespiratory cycle, one of the major pathways of plant primary metabolism, results in severe air-sensitivity of the respective mutants with the exception of the peroxisomal enzyme hydroxypyruvate reductase, HPR1, due to the existence of a second hydroxypyruvate reductase, HPR2, in the cytosol, overview. The enzyme provides a cytosolic bypass to the photorespiratory core cycle in Arabidopsis thaliana
physiological function
-
deletion of isoform HPR3 results in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype.The combined deletion of of isoforms HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1hpr2 double mutant. Isoform HPR3 could provide a compensatory bypass for the reduction of hydroxypyruvate and glyoxylate within the chloroplast
physiological function
hydroxypyruvate reductase activity is important in the recycling of metabolites derived during photorespiration; hydroxypyruvate reductase activity is important in the recycling of metabolites derived during photorespiration; hydroxypyruvate reductase activity is important in the recycling of metabolites derived during photorespiration
physiological function
upregulation of glyoxylate reductase/hydroxypyruvate reductase is associated with intestinal epithelial cells apoptosis in trinitrobenzenesulfonic acid-induced colitis
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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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
50000
-
gel filtration, two enzymes in low and high salt fractions after DEAE-cellulose chromatography
38000
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
1 * 50000, SDS-PAGE, two enzymes in low and high salt fractions after DEAE-cellulose chromatography
dimer
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
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
-
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
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
-
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
-
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
construction of hpr1 knockout and hpr2 knockout. Deletion of HPR2 results in elevated levels of hydroxypyruvate and other metabolites in leaves, photosynthetic gas exchange is slightly altered, especially under long-day conditions. Deletion of HPR1 does not show a severe phenotype, overview. The combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants and alters steady state metabolite profiles, phenotypes, overview. The most prominent naturally occuring mutation causes the decrease in Ala content coupled with enhanced levels of Arg, Asn, and Asp in the hpr1 mutant and the double knockout plant; HPR1 knockout plants show slight visually noticeable impairments in air. Under shorter daylengths of 8 h, somewhat slower growth of the hpr1 mutants than of the wild-type, in combination with an approximately 4-week delay in bolting. Combined deletion of both HPR1 and HPR2 (EC 1.1.1.81) results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is slowly lost on storage at -15°C interspersed with frequent thawing and re-freezing, about 20% activity is lost over 8 cycles of freezing and thawing
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-HCl, pH 7.5, 10% glycerol, 1 mM dithiothreitol, 2 months, 10% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Resource Q column chromatography and Superose 12 column chromatography
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 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
-
Resource Q column chromatography and Superose 12 column chromatography
Resource Q column chromatography and Superose 12 column chromatography
-
Resource Q column chromatography and Superose 12 column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli Turner (DE3); expressed in host strain to create the new strain Methylobacterium sp. MB201, 2fold increase in glyoxylate production
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE
-
expressed in Escherichia coli; recombinant expression of GFP-tagged HPR2 in transgenic Arabidospsis thaliana plants
gene GRHPR, localization of chromosome 9q12, DNA and amino acid sequence determination and analysis, genetic structure and promoter analysis, expression analysis, expression as GFP-fusion protein in the cytosol of HEK293 cells, co-expression with PPARalpha in HepG2 cells and regulation, overview
-
gene HPR3, sequence comparisons of GLYR genes and HPR genes
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
promoter region of AtHPR1 is characterized. Promoter contains the core motif of the dehydration-responsive cis-acting element and AtHPR1 expression is inducible by drought stress
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
conditional and specific down-regulation of farnesyltransferase in canola using the AtHPR1 promoter driving an RNAi construct results in yield protection against drought stress in the field
synthesis
synthesis
-
potential application in the enzymatic synthesis of glyoxylate
synthesis
-
potential application in the enzymatic synthesis of glyoxylate
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kleczkowski, L.A.; Randall, D.D.; Edwards, G.E.
Oxalate as a potent and selective inhibitor of spinach (Spinacia oleracea) leaf NADPH-dependent hydroxypyruvate reductase
Biochem. J.
276
125-127
1991
Spinacia oleracea
brenda
Chistoserdova, L.V.; Lidstrom, M.E.
Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1
J. Bacteriol.
173
7228-7232
1991
Methylorubrum extorquens AM1
brenda
Hagishita, T.; Yoshida, T.; Izumi, Y.; Mitsunaga, T.
Immunological characterization of serine-glyoxylate aminotransferase and hydroxypyruvate reductase from a methylotrophic bacterium, Hyphomicrobium methylovorum GM2
FEMS Microbiol. Lett.
142
49-52
1996
Cucumis sativus, Hyphomicrobium methylovorum GM2, Methylobacterium organophilum, Methylorubrum extorquens AM1, Spinacia oleracea
brenda
Yoshida, T.; Yamaguchi, K.; Hagishata, T.; Miyata, T.; Tanabe, T.; Toh, H.; Oshiro, T.; Shimao, M.; Itumi, Y.
Cloning and expression of the gene for hydroxypyruvate reductase (D-glycerate dehydrogenase) from an obligate methylotroph Hyphomicrobium methyovorum GM2
Eur. J. Biochem.
223
727-732
1994
Hyphomicrobium methylovorum GM2
brenda
Oliver, M.J.; Ferguson, D.L.; Burke, J.J.; Velten, J.
Inhibition of tobacco NADH-hydroxypyruvate reductase by expression of a heterologous antisense RNA derived from a cucumber cDNA: implications for the mechanism of action of antisense RNAs
Mol. Gen. Genet.
239
425-434
1993
Nicotiana tabacum cv. SR1
brenda
Kleczkowski, L.A.; Edwards, G.E.; Blackwell, R.D.; Lea, P.J.; Givan, C.V.
Enzymology of the reduction of hydroxypyruvate and glyoxylate in a mutant of barley lacking peroxisomal hydroxypyruvate reductase
Plant Physiol.
94
819-825
1990
Hordeum vulgare
brenda
Krema, C.; Lidstrom, M.E.
Hydroxypyruvate reductase from Methylobacterium extorquens AM1
Methods Enzymol.
188
373-378
1990
Methylorubrum extorquens AM1
-
brenda
Kleczkowski, L.A.; Edwards, G.E.
Identification of hydroxypyruvate and glyoxylate reductase in maize leaves
Plant Physiol.
91
278-288
1989
Zea mays
brenda
Murray, A.J.S.; Blackwell, R.D.; Lea, P.J.
Metabolism of hydroxypyruvate in a mutant of barley lacking NADH-dependent hydroxypyruvate reductase, an important photorespiratory enzyme activity
Plant Physiol.
91
395-400
1989
Hordeum vulgare
brenda
Sautter, C.; Sautter, E.; Hock, B.
Import of peroxisomal hydroxypyruvate reductase into glyoxysomes
Planta
176
149-158
1988
Citrullus lanatus subsp. vulgaris, Cucurbita pepo, Spinacia oleracea
brenda
Kleczkowski, L.A.; Givan, C.V.; Hodgson, J.M.; Randall, D.D.
Subcellular location of NADPH-dependent hydroxypyruvate reductase activity in leaf protoplasts of Pisum sativum L. and its role in photorespiratory metabolism
Plant Physiol.
88
1182-1185
1988
Pisum sativum, Spinacia oleracea
brenda
Kleczkowski, L.A.; Randall, D.D.
Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases
Biochem. J.
250
145-152
1988
Spinacia oleracea
brenda
Bamforth, C.W.; Quayle, J.R.
Hydroxypyruvate reductase activity in Paracoccus denitrificans
J. Gen. Microbiol.
101
259-267
1977
Paracoccus denitrificans
-
brenda
Feld, R.D.; Sallach, H.J.
Comparison of D-glycerate dehydrogenases from beef liver, beef spinal cord and hog spinal cord
Arch. Biochem. Biophys.
166
417-425
1975
Bos taurus, Sus scrofa
brenda
Feld, R.D.; Sallach, H.J.
D-Glycerate dehydrogenase from hog spinal cord
Methods Enzymol.
41B
289-293
1975
Sus scrofa
brenda
Sugimoto, E.; Kitagawa, Y.; Hirose, M.; Chiba, H.
Mechanisms of inhibition and activation of beef liver D-glycerate dehydrogenase by inorganic anions
J. Biochem.
72
1317-1325
1972
Bos taurus
brenda
Sugimoto, E.; Kitagawa, Y.; Nakanishi, K.; Chiba, H.
Purification and properties of beef liver D-glycerate dehydrogenase
J. Biochem.
72
1307-1315
1972
Bos taurus
brenda
Uhr, M.L.; Sneddon, M.K.
Glycine and serine inhibition of D-glycerate dehydrogenase and 3-phosphoglycerate dehydrogenase of rat brain
FEBS Lett.
17
137-140
1971
Rattus norvegicus
brenda
Kohn, L.D.; Jakoby, W.B.
Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase)
J. Biol. Chem.
243
2494-2499
1968
Delftia acidovorans
brenda
Kohn, L.D.; Jakoby, W.B.
Hydroxypyruvate reductase (D-glycerate dehydrogenase; crystalline) Pseudomonas
Methods Enzymol.
9
229-232
1966
Delftia acidovorans
-
brenda
Coderch, R.; Lluis, C.; Bozal, J.
Effect of salts on D-glycerate dehydrogenase kinetic behavior
Biochim. Biophys. Acta
566
21-31
1979
Bos taurus
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, Mus musculus
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
Shen, P.H.; Wu, B.
Over-expression of a hydroxypyruvate reductase in Methylobacterium sp. MB200 enhances glyoxylate accumulation
J. Ind. Microbiol. Biotechnol.
34
657-663
2007
Methylobacterium sp., Methylobacterium sp. MB200
brenda
Piotrowska, A.; Czerpak, R.
Cellular response of light/dark-grown green alga Chlorella vulgaris Beijerinck (Chlorophyceae) to exogenous adenine- and phenylurea-type cytokinins
Acta Physiol. Plant.
31
573-585
2009
Chlorella vulgaris
-
brenda
Timm, S.; Nunes-Nesi, A.; Paernik, T.; Morgenthal, K.; Wienkoop, S.; Keerberg, O.; Weckwerth, W.; Kleczkowski, L.A.; Fernie, A.R.; Bauwe, H.
A cytosolic pathway for the conversion of hydroxypyruvate to glycerate during photorespiration in Arabidopsis
Plant Cell
20
2848-2859
2008
Arabidopsis thaliana, Arabidopsis thaliana (Q9C9W5), Arabidopsis thaliana (Q9CA90)
brenda
Wang, Y.; Beaith, M.; Chalifoux, M.; Ying, J.; Uchacz, T.; Sarvas, C.; Griffiths, R.; Kuzma, M.; Wan, J.; Huang, Y.
Shoot-specific down-regulation of protein farnesyltransferase (alpha-subunit) for yield protection against drought in canola
Mol. Plant
2
191-200
2009
Brassica napus
brenda
Timm, S.; Florian, A.; Jahnke, K.; Nunes-Nesi, A.; Fernie, A.R.; Bauwe, H.
The hydroxypyruvate-reducing system in Arabidopsis: multiple enzymes for the same end
Plant Physiol.
155
694-705
2011
Arabidopsis thaliana (Q9LE33)
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 (A0A1I9LPQ6), Arabidopsis thaliana (Q9C9W5), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LE33)
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 (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
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