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Enzyme Nomenclature
Information on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.298
Word Map on EC 1.1.1.298
- 1.1.1.298
- acetyl-coa
- aurantiacus
- chloroflexus
-
autotrophic
- metallosphaera
- sedula
-
3-hydroxypropionate/4-hydroxybutyrate
-
malonyl-coenzyme
-
nadph-dependent
-
acetyl-coenzyme
- propionyl-coa
- succinyl-coa
- sulfolobales
-
acrylic
- crenarchaeota
-
polyhydroxyalkanoate
- tokodaii
- 3-hydroxypropionyl-coa
-
transhydrogenase
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.298
-
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RECOMMENDED NAME
GeneOntology No.
3-hydroxypropionate dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
150386-09-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
metabolism
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the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
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physiological function
-
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
physiological function
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enzyme is part of an autotrophic 3-hydroxypropionate/4-hydroxybutyrate carbon dioxide assimilation pathway in Metallospaera sedula. In the pathway, CO2 is fixed with acetyl-CoA/propionyl-CoA carboxylase as key carboxylating enzyme. One acetyl-CoA and two bicarbonate molecules are reductively converted via 3-hydroxypropionate to succinyl-CoA
physiological function
the organism assimilates CO2 by the 3-hydroxypropionate cycle, and malonyl-CoA reductase is an essential enzyme for the cycle
physiological function
-
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
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physiological function
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the organism assimilates CO2 by the 3-hydroxypropionate cycle, and malonyl-CoA reductase is an essential enzyme for the cycle
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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
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
-
-
-
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
-
spectrophotometric product determination
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r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
-
-
?
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, additionally exhibits 3-hydroxypropionate dehydrogenase activity
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-
?
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
-
-
-
r
malonate semialdehyde + NADH + H+
3-hydroxypropanoate + NAD+
NADH can partially substitute (20% activity) for NADPH
-
-
?
malonate semialdehyde + NADH + H+
3-hydroxypropanoate + NAD+
NADH can partially substitute (20% activity) for NADPH
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
NADH can partially substitute (20% activity) for NADPH
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
NADH can partially substitute (20% activity) for NADPH
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
-
-
?
additional information
?
-
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
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-
-
additional information
?
-
-
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives
-
-
-
additional information
?
-
-
enzyme is part of an autotrophic CO2 fixation pathway in which acetyl-CoA is carboxylated and reductively converted via 3-hydroxypropionate to propionyl-CoA. Propionyl-CoA is carboxylated and converted via succinyl-CoA and CoA transfer to malyl-CoA. Malyl-CoA is cleaved to acetyl-CoA and glyoxylate. Thereby, the first CO, acceptor molecule acetyl-CoA is regenerated, completing the cycle and the net CO, fixation product glyoxylate is released
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-
-
additional information
?
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-
bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
-
-
-
additional information
?
-
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
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-
-
additional information
?
-
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
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-
-
additional information
?
-
succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
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-
-
additional information
?
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succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
-
-
-
r
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
-
-
-
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Q5SLQ6
-
-
-
?
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q5SLQ6
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
A4YI81
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
A4YI81
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
Q6QQP7
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
Q6QQP7
-
-
-
?
additional information
?
-
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
-
-
-
additional information
?
-
-
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives
-
-
-
additional information
?
-
-
enzyme is part of an autotrophic CO2 fixation pathway in which acetyl-CoA is carboxylated and reductively converted via 3-hydroxypropionate to propionyl-CoA. Propionyl-CoA is carboxylated and converted via succinyl-CoA and CoA transfer to malyl-CoA. Malyl-CoA is cleaved to acetyl-CoA and glyoxylate. Thereby, the first CO, acceptor molecule acetyl-CoA is regenerated, completing the cycle and the net CO, fixation product glyoxylate is released
-
-
-
additional information
?
-
Q6QQP7
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
-
-
-
additional information
?
-
Q6QQP7
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
-
no metal ion requirement; no metal ion requirement, no effects by 0.2 mM MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4; up to 0.2 mM, no effect on activity: MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4
additional information
addition of Zn2+ (0-0.04 mM) or Mg2+or Mn2+(0-5 mM) to the enzyme assay mixture neither stimulates nor inactivates the enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibitory: EDTA and ethylene glykol, up to 0.2 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetic analysis, overview; steady-state kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 45
-
90% of maximal activity within this range; activity range; more than 90% of maximum activity
37 - 60
63% of maximal activity at 60°C, maximal activity at 50°C, about 30% at 37°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
low activity in heterotrophically-grown cell
-
low activity in heterotrophically-grown cell
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
3 min, about 40% residual activity; 3 min, purified enzyme, significant denaturation and inactivation; purified enzyme, 30 min, partial denaturation
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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
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21; MmsB gene, overexpression in Escherichia coli strain BL21, subcloning in strain DH5alpha
-
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
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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
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
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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-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.298)
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