Information on EC 1.1.1.81 - hydroxypyruvate reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
1.1.1.81
-
RECOMMENDED NAME
GeneOntology No.
hydroxypyruvate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
formaldehyde assimilation I (serine pathway)
-
Glycine, serine and threonine metabolism
-
Glyoxylate and dicarboxylate metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NADP+ 2-oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
At1g12550
Q9LE33
gene name
AtHPR1
-
-
beta-hydroxypyruvate reductase
-
-
-
-
D-2-hydroxy-acid dehydrogenase
-
-
D-glycerate dehydrogenase
-
-
-
-
glyoxylate reductase/hydroxypyruvate reductase
-
-
HPR1
Q9C9W5, Q9CA90
-
hydroxypyruvate reductase
Q9C9W5
-
NADH-dependent hydroxypyruvate reducing enzyme activity
-
-
NADH-dependent hydroxypyruvate reductase
-
-
NADH-HPR
-
-
NADH:hydroxypyruvate reductase
-
-
-
-
NADPH-dependent hydroxypyruvate reductase
Q9CA90
-
hydroxypyruvate reductase
-
-
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)
CAS REGISTRY NUMBER
COMMENTARY
9059-44-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
HPR2; gene At1g79870 encodes isozyme HPR2
UniProt
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
Hyphomicrobium methylovorum GM2
-
-
-
Manually annotated by BRENDA team
strain MB200, capable of producing glyoxylate from methanol
-
-
Manually annotated by BRENDA team
strain MB200, capable of producing glyoxylate from methanol
-
-
Manually annotated by BRENDA team
gene GRHPR
-
-
Manually annotated by BRENDA team
Nicotiana tabacum cv. SR1
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
NADH-HPR is extensively involved in carbon metabolism
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
-, Q9C9W5, Q9CA90
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
Q9LE33
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-butandione + NAD(P)H
butan-2-ol-3-one + NAD(P)+
show the reaction diagram
-
33 mM, 12% of activity with hydroxypyruvate
-
?
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
show the reaction diagram
-
33 mM, 14% of activity with hydroxypyruvate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
activity with hydroxypyruvate and NADPH is 2fold higher than with other pair of reactants
-
ir
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
33 mM, 15% activity
-
-
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
cofactor NADH, 15% of activity with hydroxypyruvate, cofactor NADPH, 1.5% of activity with hydroxypyruvate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
glyoxylate + NAD(P)H + H+
glycolate + NAD(P)+
show the reaction diagram
-, Q9C9W5, Q9CA90
-
-
-
?
glyoxylate + NADH
glycolate + NAD+
show the reaction diagram
-
-
-
-
?
glyoxylate + NADPH
glycolate + NADP+
show the reaction diagram
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
Q9LE33
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?, r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?, ir
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
Methylobacterium organophilum, Hyphomicrobium methylovorum GM2
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
Hyphomicrobium methylovorum GM2
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
Nicotiana tabacum cv. SR1
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
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)+
show the reaction diagram
Methylobacterium organophilum XX
-
-
-
?
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
show the reaction diagram
-, Q9C9W5, Q9CA90
-
-
-
?
hydroxypyruvate + NADH
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
-, Q9C9W5, Q9CA90
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
Q9LE33
-
-
-
-
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
-
-, key enzyme of the serine cycle
-
-
?
oxaloacetate + NAD(P)H
malate + NAD(P)+
show the reaction diagram
-
33 mM, 32% of activity with hydroxypyruvate
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
-
-, key enzyme of the serine cycle
-
-
?
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
-
-
-
additional information
?
-
-
structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
Q9LE33
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
Methylobacterium organophilum, Hyphomicrobium methylovorum GM2
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
Hyphomicrobium methylovorum GM2
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
-
-
-
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
Nicotiana tabacum cv. SR1
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+
show the reaction diagram
-
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)+
show the reaction diagram
Methylobacterium organophilum XX
-
-
-
?
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
show the reaction diagram
-, Q9C9W5, Q9CA90
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
-
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
show the reaction diagram
Q9LE33
-
-
-
-
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
show the reaction diagram
-
key enzyme of the serine cycle
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADH
-
dependent on
NADH
-, Q9C9W5, Q9CA90
; 4fold lower activity with HPR2 compared to NADPH
NADPH
-
binding structure
NADPH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
-, Q9C9W5, Q9CA90
preferred cofactor of HPR2; shows some reactivity with NADPH
NADPH
Q9LE33
NADPH is preferred over NADH
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
Ag+
-
0.1 mM, complete inhibition
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
bromide
-
33 mM, 38% inhibition
bromide
-
100 mM, 70% inhibition of D-glycerate oxidation
citrate
-
5 mM, 20% inhibition of NADH linked hydroxypyruvate reduction, 25% of NADPH linked reduction
citrate
-
competitive vs. hydroxypyruvate
Cl-
-
100 mM, 50% inhibition of D-glycerate oxidation
CTP
-
1 mM, 73% and 71% inhibition of liver and spinal cord enzyme respectively
D-glycerate
-
5 mM, 20% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction
D-glycerate
-
the enzyme shows product inhibition
glycolate
-
5 mM, 15% of NADPH linked reduction
glyoxylate
-
10 mM, 55% inhibition of NADH linked hydroxypyruvate reduction, 15% of NADPH linked reduction, 80% of NAD+ linked glycerate oxidation
GTP
-
1 mM, 94% and 93% inhibition of liver and spinal cord enzyme respectively
Hg2+
-
0.1 mM, complete inhibition
Hydroxypyruvate
-
0.5 mM, 90% of NAD+ linked glycerate oxidation
Hydroxypyruvate
-
2 mM, 79% inhibition of enzyme activity in LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
Hydroxypyruvate
-
substrate inhibition at high concentrations
Iodide
-
33 mM, 39% inhibition
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
NaNO3
-
80 mM, 50% inhibition
NO3-
-
100 mM, 87% inhibition of D-glycerate oxidation
oxalate
-
2 mM, 90% inhibition
oxalate
-, Q9C9W5, Q9CA90
; strong inhibition of HPR2
oxaloacetate
-
2.5 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 20% of NADPH linked reduction
p-chloromercuribenzoate
-
0.1 mM, complete inhibition
Phosphohydroxypyruvate
-
2 mM, 44-71% inhibition
Phosphohydroxypyruvate
-
0.025 mM, 66% and 64% inhibition of liver and spinal cord enzyme respectively
pyruvate
-
10 mM, 40% inhibition of NADH linked hydroxypyruvate reduction
pyruvate
-
1 mM, 73% and 89% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
SO42-
-
100 mM, 55% inhibition of D-glycerate oxidation
Sodium bisulfite
-
0.01 mM, 16% inhibition, 0.1 mM, 67% inhibition
Tartronate
-
2 mM, 30-55% inhibition
Tartronate
-
2 mM, 83% inhibition of enzyme activity in LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
UTP
-
1 mM, 83% and 84% inhibition of liver and spinal cord enzyme respectively
Iodide
-
100 mM, 90% inhibition of D-glycerate oxidation
additional information
-
not inhibited by 2 mM acetohydroxamate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Br-
-
100 mM, 10fold activation of hydroxypyruvate reduction
Br-
-
2fold activation
Cl-
-
100 mM, 9fold activation of hydroxypyruvate reduction
Cl-
-
2fold activation
CsCl
-
80 mM, 3fold increase in hydroxypyruvate reductase activity
F-
-
100 mM, 67% activation of hydroxypyruvate reduction
I-
-
100 mM, 9fold activation of hydroxypyruvate reduction
I-
-
2.5fold activation
KCl
-
80 mM, 9fold increase in hydroxypyruvate reductase activity
N,N'-diphenylurea
-
-
-
N6-benzyladenine
-
-
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
NO3-
-
100 mM, 8fold activation of hydroxypyruvate reduction
NO3-
-
2fold activation
SO42-
-
100 mM, 3fold activation of hydroxypyruvate reduction
SO42-
-
2fold activation
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.522
-
D-glycerate
-
D-glycerate oxidation, 50 mM, NaCl, pH 9
1.4
-
DL-glycerate
-
-
0.0038
-
Hydroxypyruvate
-
value increases with NaCl concentrations higher than 10 mM
0.004
-
Hydroxypyruvate
-
-
0.08
-
Hydroxypyruvate
-
enzyme activity of wild-type in 40-60% precipitate fractions after ammonium sulfate fractionation
0.1
-
Hydroxypyruvate
-
cofactor NADH
0.1
-
Hydroxypyruvate
-
-
0.11
-
Hydroxypyruvate
-
ammonium sulfate fractionated leaf extracts, 45-60% fraction
0.13
-
Hydroxypyruvate
-
with 0.15 mM NADPH
0.13
-
Hydroxypyruvate
-
-
0.175
-
Hydroxypyruvate
Hyphomicrobium methylovorum GM2
-
native enzyme
0.189
-
Hydroxypyruvate
Hyphomicrobium methylovorum GM2
-
purified recombinant enzyme
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
0.8
-
Hydroxypyruvate
-
at pH 6.0
1.25
-
Hydroxypyruvate
-
cofactor NADPH
2.1
-
Hydroxypyruvate
-
with 0.15 mM NADH
2.1
-
Hydroxypyruvate
-
-
10
-
Hydroxypyruvate
-
enzyme in high-salt fraction of DEAE-cellulose chromatography
40
-
Hydroxypyruvate
-
enzyme in low-salt fraction of DEAE-cellulose chromatography
0.077
-
NAD+
-
-
0.22
-
NAD+
-
D-glycerate oxidation, 50 mM, NaCl, pH 9
0.0061
-
NADH
-
-
0.013
-
NADH
-
with hydroxypyruvate as substrate, pH 7.5
0.015
-
NADH
-
with glyoxylate as substrate, pH 7.5
0.055
-
NADH
Hyphomicrobium methylovorum GM2
-
native enzyme
0.064
-
NADH
Hyphomicrobium methylovorum GM2
-
purified recombinant enzyme
0.112
-
NADH
-
-
0.037
-
NADP+
-
-
0.015
-
NADPH
-
-
0.018
-
NADPH
-
-
0.021
-
NADPH
-
with glyoxylate as substrate, pH 7.5
0.025
-
NADPH
-
with hydroxypyruvate as substrate, pH 7.5
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.1
-
NADH
-
with hydroxypyruvate as substrate, pH 7.5
11
-
NADH
-
with glyoxylate as substrate, pH 7.5
1.8
-
NADPH
-
with hydroxypyruvate as substrate, pH 7.5
2.4
-
NADPH
-
with glyoxylate as substrate, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
0.068
-
-
enzyme activity in leaf extracts of wild type
0.077
-
-
oxidation of glycerate
0.0834
-
-
enzyme activity in crude leaf extracts of wild type
0.1
-
-
in cell-free extracts
0.135
-
-
cofactor NADH
0.33
-
-
cofactor NADPH
0.745
-
-
-
0.9
-
-
in cell-free extracts
1.06
-
-
ammonium sulfate fractionated leaf extracts, 45-60% fraction
1.5
-
-
in cell-free extracts
1.7
-
-
in cell-free extracts
1.9
-
Hyphomicrobium methylovorum GM2
-
in cell-free extracts
2.67
-
-
-
13.01
-
Nicotiana tabacum cv. SR1
-
enzyme activity in leaf tissue
104.8
-
-
-
943
-
Hyphomicrobium methylovorum GM2
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
broad optimum between pH 4.0 and 6.5 for hydroxypyruvate reduction
5
-
-
sharp peak
5.3
-
-
sharp drop of activity below and above
6.2
-
-
assay at
6.5
-
-
hydroxypyruvate reduction
7
-
-
hydroxypyruvate reduction
7.5
-
-
assay at
9
11
-
glycerate oxidation
9.3
-
-
D-glycerate oxidation
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
-
sharp drop of activity below and above
5.5
6
-
strong decrease above
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Nicotiana tabacum cv. SR1
-
-
Manually annotated by BRENDA team
-
mainly localized in bundle sheet cells
Manually annotated by BRENDA team
-, Q9C9W5, Q9CA90
; both HPR1 and HPR2 (EC 1.1.1.81) are the major hydroxypyruvate-reducing enzymes in leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
about 70% of NADPH-dependent hydroxypyruvate reductase activity is localized in the cytosol, minor activities in chlorplasts and peroxisomes
Manually annotated by BRENDA team
-, Q9C9W5, Q9CA90
HPR2
Manually annotated by BRENDA team
-, Q9C9W5, Q9CA90
HPR!
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-
immunoprecipitation
50000
-
-
gel filtration, two enzymes in low and high salt fractions after DEAE-cellulose chromatography
70000
-
-
gel filtration
71000
-
-
gradient PAGE
72000
-
-
sedimentation velocity analysis
76500
-
-
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 34000, SDS-PAGE
?
-, Q9C9W5, Q9CA90
x * 43200, HPR2, SDS-PAGE
?
-
x * 34000, SDS-PAGE
-
dimer
-
2 * 37000, SDS-PAGE
dimer
-
2 * 38000, SDS-PAGE
dimer
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
monomer
-
1 * 50000, SDS-PAGE, two enzymes in low and high salt fractions after DEAE-cellulose chromatography
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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, 18C, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
-
-
half-life of 35 min in 50 mM phosphate buffer, pH 7.0
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dithiothreitol stabilizes
-
activity is slowly lost on storage at -15C interspersed with frequent thawing and re-freezing, about 20% activity is lost over 8 cycles of freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 50 mM Tris-HCl, pH 7.5, 10% glycerol, 1 mM dithiothreitol, 2 months, 10% loss of activity
-
-20C, 20 mM MOPS, pH 7.1, 14 mM 2-mercaptoethanol, 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
recombinant His-tag protein from Escherichia coli
-
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 protein from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli; recombinant expression of GFP-tagged HPR2 in transgenic Arabidospsis thaliana plants
-, Q9C9W5, Q9CA90
expression in Escherichia coli
Q9LE33
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
expressed in Escherichia coli
Hyphomicrobium methylovorum GM2
-
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
-
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
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q9C9W5, Q9CA90
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
potential application in the enzymatic synthesis of glyoxylate
synthesis
-
potential application in the enzymatic synthesis of glyoxylate
-