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Information on EC 1.1.1.81 - hydroxypyruvate reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LE33
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EC Tree
1.1.1.81 hydroxypyruvate reductaseSpecify your search results
Word Map
- 1.1.1.81
- peroxisomal
-
photorespiration
-
photorespiratory
- microbodies
- glyoxysomes
- hyphomicrobium
-
pumpkin
-
hexulose
- extorquens
- methylovorum
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hydroxypyruvate reductase, nadh-hpr, athpr1, nadph-dependent hydroxypyruvate reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HPR3
beta-hydroxypyruvate reductase
-
-
-
-
D-glycerate dehydrogenase
-
-
-
-
HPR1
HPR2
hydroxypyruvate reductase
NADH:hydroxypyruvate reductase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NADP+ 2-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
9059-44-3
-
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
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
-
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
-
-
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
reaction of EC 1.1.1.237
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
low activity
-
-
?
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 + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
best substrate
-
-
r
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
-
-
?
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
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
?
-
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
?
-
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 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
?
-
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
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
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+
-
-
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
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
?
-
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 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
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
isoform HPR3 prefers NADPH over NADH
NADPH
isoform HPR3 prefers NADPH over NADH
NADH
isoform HPR1 prefers NADH over NADPH
NADH
isoform HPR2 prefers NADPH over NADH
NADPH
isoform HPR1 prefers NADH over NADPH
NADPH
isoform HPR2 prefers NADPH over NADH
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
4-hydroxyphenylpyruvate
pH 7.0, 30°C, recombinant enzyme
6.1
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.122
4-hydroxyphenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.927
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.153
4-hydroxyphenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.232
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
both HPR1 and HPR2 (EC 1.1.1.81) are the major hydroxypyruvate-reducing enzymes in leaves
additional information
quantitative reverse transcription PCR enzyme expression analysis
additional information
quantitative reverse transcription PCR enzyme expression analysis
additional information
-
quantitative reverse transcription PCR enzyme expression analysis
additional information
RT-PCR enzyme expression analysis, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deletion of 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 HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. HPR mutants show impaired growth and contain less chlorophyll, phenotypes, detailed overview
physiological function
evolution
malfunction
metabolism
in vitro characterization of the recombinant proteins reveals that HPPR2 has both hydroxypyruvate reductase (HPR EC 1.1.1.81, main activity) and hydroxyphenylpyruvate reductase (HPPR, EC 1.1.1.237) activities, whereas HPPR3 has a strong preference for pHPP, and both enzymes are localized in the cytosol. In Arabidopsis thaliana, HPPR2 and HPPR3, together with tyrosine aminotransferase 1 (TAT1), constitute to a probably conserved biosynthetic pathway from tyrosine to 4-hydroxyphenyllactic acid (pHPL), from which some specialized metabolites, such as rosmarinic acid (RA), can be generated in specific groups of plants. Role of HPPR in the tyrosine conversion pathway, overview
physiological function
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
HPR3 is the third enzyme in Arabidopsis (Arabidopsis thaliana), which also reduces 4-hydroxypyruvate (HP) to glycerate and shows even more activity with glyoxylate, a more upstream intermediate of the photorespiratory cycle. In silico analysis and proteomic studies target HPR3 to the chloroplast, the enzyme might provide a compensatory bypass for the reduction of HP and glyoxylate within this compartment
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
evolution
HPR1 and HPR2 are the major hydroxypyruvate-reducing enzymes in leaves
evolution
no hydroxyphenylpyruvate reductase (HPPR) activity by isozyme HPPR4 from Arabidopsis thaliana. Isozyme HPPR2 mainly shows hydroxypyruvate reductase (HPR) activity, while isozyme HPPR3 mainly shows 4-hydroxyphenylpyruvate reductase (EC 1.1.1.237) activity. Enzyme HPPR2 belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, group II
malfunction
Arabidopsis thaliana mutants defective in either HPPR2 or HPPR3 isozyme contain lower amounts of pHPL and are impaired in conversion of tyrosine to pHPL. Furthermore, a loss-of-function mutation in tyrosine aminotransferase (TAT) also reduces the pHPL accumulation in plants
malfunction
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. Otherwise, the mutant closely resembles wild-type plants. The combined deletion of both HPR1 and HPR2 results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
malfunction
deletion of photorespiratory enzymes typically leads to a strong air sensitivity of the respective mutants, which can be fully recovered by elevated-CO2 conditions. While this is a distinctive feature of most photorespiratory mutants, Arabidopsis thaliana HPR1 knockout mutants grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
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
hydroxypyruvate reductase activity is important in the recycling of metabolites derived during photorespiration
physiological function
Arabidopsis mutants defective in either isoform HPPR2 or HPPR3 contain lower amounts of 4-hydroxyphenyllactic acid and are impaired in conversion of tyrosine to 4-hydroxyphenyllactic acid
physiological function
hydroxyphenylpyruvate reductase (HPPR), which catalyzes the reduction of 4-hydroxyphenylpyruvic acid (pHPP) to 4-hydroxyphenyllactic acid (pHPL), is the key enzyme in the biosynthesis of rosmarinic acid (RA) from tyrosine and, so far, HPPR activity is reported only from the RA-accumulating plants
physiological function
the enzyme activity shows that photorespiratory metabolism is not confined to chloroplasts, peroxisomes, and mitochondria but also extends to the cytosol. The extent to which cytosolic reactions contribute to the operation of the photorespiratory cycle in varying natural environments might be dynamically regulated by the availability of NADH in the context of peroxisomal redox homeostasis. But isozyme HPR1 plays the dominant role in photorespiration
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HPR3_ARATH
323
0
34912
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme contains a D-isomer-specific 2-hydroxyacid dehydrogenase domain
additional information
-
the enzyme contains a D-isomer-specific 2-hydroxyacid dehydrogenase domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
deletion of HPR3 by T-DNA insertion mutagenesis resulting 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 HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. Generation of two independent T-DNA insertion lines for the gene At1g12550, i.e. hpr3-1 and hpr3-2
additional information
deletion of HPR3 by T-DNA insertion mutagenesis resulting 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 HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. Generation of two independent T-DNA insertion lines for the gene At1g12550, i.e. hpr3-1 and hpr3-2
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
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
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
additional information
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
additional information
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
additional information
-
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
additional information
deletion of HPR2 by T-DNA insertion, HPR2 knockout plants do not show visually noticeable impairments in air, but combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants. Crossing of hpr1-1 and hpr2-1 leads to functional inactivation of both genes. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles and photorespiratory 13C fluxes. The leaf glycerate content remains essentially unaltered in the hpr2 mutant and is increased in hpr1 and the double knockout plant. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
additional information
-
deletion of HPR2 by T-DNA insertion, HPR2 knockout plants do not show visually noticeable impairments in air, but combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants. Crossing of hpr1-1 and hpr2-1 leads to functional inactivation of both genes. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles and photorespiratory 13C fluxes. The leaf glycerate content remains essentially unaltered in the hpr2 mutant and is increased in hpr1 and the double knockout plant. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
additional information
-
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
additional information
generation of Arabidopsis thaliana HPR1 knockout mutants, which grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
additional information
generation of Arabidopsis thaliana HPR1 knockout mutants, which grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rose-gami B (DE3) by nickel affinity chromatography and desalting gel filtration
recombinant tagged enzyme HPR2 from hpr1-knockout mutant Arabidopsis thaliana strain by ammonium sulfate fractionation, ion-exchange and affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene HPR3, At1g12550, genetic structure and RT-PCR expression analysis
gene HPR2, At1g70870, recombinant expression of tagged HPR2 in a hpr1-knockout mutant Arabidopsis thaliana strain, RT-PCR enzyme expression analysis
gene HPR3, sequence comparisons of GLYR genes and HPR genes
isozyme HPPR2, sequence comparisons and phylogenetic analysis, quantitative reverse transcription PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rose-gami B (DE3). Recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana protoplasts
recombinant expression of GFP-tagged HPR2 in transgenic Arabidospsis thaliana plants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9C9W5), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana
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)
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)
Xu, J.; Fang, X.; Li, C.; Zhao, Q.; Martin, C.; Chen, X.; Yang, L.
Characterization of Arabidopsis thaliana hydroxyphenylpyruvate reductases in the tyrosine conversion pathway
Front. Plant Sci.
9
1305
2018
Arabidopsis thaliana (A0A178WMD4), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9CA90)
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 (Q9CA90), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9CA90)
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 (Q9CA90), Arabidopsis thaliana (Q9LE33), Arabidopsis thaliana Col-0 (Q9CA90), Arabidopsis thaliana Col-0 (Q9LE33)
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