Information on EC 1.1.1.81 - hydroxypyruvate reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9CA90

for references in articles please use BRENDA:EC1.1.1.81
Word Map on EC 1.1.1.81
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9CA90


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Arabidopsis thaliana

EC NUMBER
COMMENTARY hide
1.1.1.81
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RECOMMENDED NAME
GeneOntology No.
hydroxypyruvate reductase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formaldehyde assimilation I (serine pathway)
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L-serine biosynthesis II
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serine metabolism
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Glycine, serine and threonine metabolism
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NADP+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9059-44-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
physiological function
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
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
show the reaction diagram
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r
glyoxylate + NAD(P)H + H+
glycolate + NAD(P)+
show the reaction diagram
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-
-
?
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
show the reaction diagram
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-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
show the reaction diagram
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?
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
show the reaction diagram
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r
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
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-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
show the reaction diagram
A0A178WMD4, A0A1I9LPQ6, Q9CA90
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r
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
show the reaction diagram
Q9C9W5, Q9CA90
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?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
show the reaction diagram
A0A178WMD4, A0A1I9LPQ6, Q9CA90
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?
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
show the reaction diagram
A0A178WMD4, A0A1I9LPQ6, Q9CA90
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r
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
Q9LE33
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?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
Q9LE33
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additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADP+
NADPH
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxalate
strong inhibition of HPR2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.1
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.232
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
both HPR1 and HPR2 (EC 1.1.1.81) are the major hydroxypyruvate-reducing enzymes in leaves
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43200
x * 43200, HPR2, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43200, HPR2, SDS-PAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of GFP-tagged HPR2 in transgenic Arabidospsis thaliana plants
expressed in Escherichia coli
expression in Escherichia coli
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gene HPR3, sequence comparisons of GLYR genes and HPR genes
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information