Information on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)

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

EC NUMBER
COMMENTARY hide
1.1.1.298
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RECOMMENDED NAME
GeneOntology No.
3-hydroxypropionate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate cycle
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3-hydroxypropanoate/4-hydroxybutanate cycle
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glyoxylate assimilation
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uracil degradation III
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CO2 fixation in Crenarchaeota
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Carbon fixation pathways in prokaryotes
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxypropionate:NADP+ oxidoreductase
Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively [1,2]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75 [3]. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.
CAS REGISTRY NUMBER
COMMENTARY hide
150386-09-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; gene MmsB; MmsB gene
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Manually annotated by BRENDA team
gene MmsB; MmsB gene
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
3-hydroxypropanoate + NAD+
malonate semialdehyde + NADH + H+
show the reaction diagram
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-
-
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r
3-hydroxypropanoate + NAD+
malonate-semialdehyde + NADH + H+
show the reaction diagram
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-
-
-
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH + H+
show the reaction diagram
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-
-
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r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
show the reaction diagram
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spectrophotometric product determination
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r
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
show the reaction diagram
malonate semialdehyde + NADH + H+
3-hydroxypropanoate + NAD+
show the reaction diagram
malonate semialdehyde + NADPH
3-hydroxypropionate + NADP+
show the reaction diagram
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-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
show the reaction diagram
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
show the reaction diagram
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
show the reaction diagram
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-
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r
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
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH + H+
show the reaction diagram
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-
-
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r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
show the reaction diagram
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-
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r
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
show the reaction diagram
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-
-
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r
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
show the reaction diagram
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
show the reaction diagram
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
show the reaction diagram
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r
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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more active with NADP+ than NAD+; NADP+ is preferred over NAD+
NADP+
NADPH
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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stimulation
Fe2+
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stimulation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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90% inhibition
Zn
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0.2 mM, 60% inhibition
Zn2+
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60% inhibition at 0.2 mM
additional information
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not inhibitory: EDTA and ethylene glykol, up to 0.2 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.8
3-hydroxypropanoate
0.07
Malonate semialdehyde
pH 7.4, 65C
2.4
NAD+
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pH 8.5, 37C; pH 8.5, 37C, recombinant enzyme
0.25
NADP+
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pH 8.5, 37C; pH 8.5, 37C, recombinant enzyme
0.07
NADPH
pH 7.4, 65C
additional information
additional information
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steady-state kinetic analysis, overview; steady-state kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
3-hydroxypropanoate
115
Malonate semialdehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0125
3-hydroxypropanoate
4480
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
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substrate 3-hydroxypropionate, pH 9.0, 45C
0.04
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substrate malonate-semialdehyde, pH 9.0, 45C
8.7
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pH 8.5, 37C
8.8
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purified recombinant enzyme, pH 8.5, 37C
10
purified recombinant enzyme, pH 7.8, 55C
200
pH 7.4, 65C, heterologously expressed enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
optimum pH at 65C
8.8 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
7 - 10
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activity range
8.2
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about 30% of maximum acticity
9
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about 65% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 45
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90% of maximal activity within this range; activity range; more than 90% of maximum activity
37 - 60
63% of maximal activity at 60C, maximal activity at 50C, about 30% at 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
gel filtration
300000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 145000, SDS-PAGE
homotrimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 45
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purified enzyme, over 90% activity remaining after 30 min
45
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30 min, purified enzyme, completely stable; 30 min, stable
55
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3 min, about 40% residual activity; 3 min, purified enzyme, significant denaturation and inactivation; purified enzyme, 30 min, partial denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is oxygen insensitive but sensitive to repeated freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, presence of 10% (vol/vol) glycerol, stable for weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 100fold by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography; recombinant enzyme from Escherichia coli strain BL21 96fold by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, followed by ultrafiltration
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recombinant enzyme from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli Rosetta 2(DE3)
expression in Escherichia coli strain BL21; MmsB gene, overexpression in Escherichia coli strain BL21, subcloning in strain DH5alpha
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gene mcr, functional expression in Escherichia coli under the T5 promoter control leading to production of 3-hydroxypropionate, coexpression with the nicotinamide nucleotide transhydrogenase that converts NADH to NADPH, required by MCR
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the specific activity of this conversion in autotrophically grown cells is 1.8 microM/min * mg protein, whereas in heterotrophically grown cells the specific activity is 0.35 microM/min * mg protein
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