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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
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photorespiration
-
photorespiratory
- microbodies
- glyoxysomes
- hyphomicrobium
-
pumpkin
-
hexulose
- extorquens
- methylovorum
- biotechnology
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hydroxypyruvate reductase, nadh-hpr, athpr1, nadph-dependent hydroxypyruvate reductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
At1g12550
beta-hydroxypyruvate reductase
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-
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D-glycerate dehydrogenase
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-
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glyoxylate reductase/hydroxypyruvate reductase
glyoxylate/hydroxypyruvate reductase
glyoxylate/hydroxypyruvate reductase A
GRHPR
HPR
HPR1
HPR2
HPR3
HRP
hydroxypyruvate reductase
LCv4_3219
MCA1407
NAD(P)H-dependent hydroxypyruvate reductase
NADH:hydroxypyruvate reductase
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-
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NADPH-dependent hydroxypyruvate reductase
additional information
GRHPR
bifunctional enzyme with glyoxylate reductase and hydroxypyruvate reductase activities
additional information
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the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
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the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
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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
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redox reaction
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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
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?
2-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
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-
-
?
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
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33 mM, 14% of activity with hydroxypyruvate
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?
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
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-
-
r
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
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-
-
?
oxaloacetate + NAD(P)H
malate + NAD(P)+
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33 mM, 32% of activity with hydroxypyruvate
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?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
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?
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
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ir
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
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-
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ir
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
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-
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ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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-
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ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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-
-
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ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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-
-
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ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
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-
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?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
reaction of EC 1.1.1.237
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?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
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?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
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the enzyme is involved in removal of the metabolic by-product from liver
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-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
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cofactor NADH, 15% of activity with hydroxypyruvate, cofactor NADPH, 1.5% of activity with hydroxypyruvate
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?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
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33 mM, 15% activity
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?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
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activity with hydroxypyruvate and NADPH is 2fold higher than with other pair of reactants
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ir
glyoxylate + NADH + H+
glycolate + NAD+
97% of the activity with 3-hydroxypyruvate
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ir
glyoxylate + NADH + H+
glycolate + NAD+
97% of the activity with 3-hydroxypyruvate
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ir
glyoxylate + NADH + H+
glycolate + NAD+
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24% of the activity with 3-hydroxypyruvate
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ir
glyoxylate + NADH + H+
glycolate + NAD+
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60% of the activity with 3-hydroxypyruvate
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ir
glyoxylate + NADH + H+
glycolate + NAD+
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60% of the activity with 3-hydroxypyruvate
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ir
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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-
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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-
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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cofactor NADPH, 80% of activity with NADH, rate of oxidation reaction: 1.5% of reduction reaction only with cofactor NADH
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r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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?, r
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
low activity
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
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?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
low activity
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
best substrate
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r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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?, r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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key enzyme of the serine cycle
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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key enzyme of the serine cycle
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?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
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?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
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?
additional information
?
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the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
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?
additional information
?
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the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
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?
additional information
?
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the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
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?
additional information
?
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the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
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?
additional information
?
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the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
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?
additional information
?
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HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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?
additional information
?
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HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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?
additional information
?
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HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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?
additional information
?
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HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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?
additional information
?
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HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
additional information
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
additional information
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
additional information
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
additional information
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
additional information
?
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isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
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-
additional information
?
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isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
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-
additional information
?
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isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
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-
additional information
?
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enzyme HPR2 shows relaxed substrate and cofactor specificity, it also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79). Irreversibility of the HPR2 reaction has been reported
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additional information
?
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enzyme HPR2 shows relaxed substrate and cofactor specificity, it also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79). Irreversibility of the HPR2 reaction has been reported
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-
additional information
?
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the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
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-
additional information
?
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the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
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-
additional information
?
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isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
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-
additional information
?
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enzyme HPR2 shows relaxed substrate and cofactor specificity, it also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79). Irreversibility of the HPR2 reaction has been reported
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additional information
?
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the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
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-
additional information
?
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the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
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-
additional information
?
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enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
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?
additional information
?
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structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
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?
additional information
?
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enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
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-
additional information
?
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enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
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-
additional information
?
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enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
-
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-
additional information
?
-
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enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
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-
additional information
?
-
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enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
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-
additional information
?
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the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
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?
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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
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
</