Any feedback?
Information on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.298Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.298 3-hydroxypropionate dehydrogenase (NADP+)IUBMB Comments
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 . Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.
Specify your search results
Word Map
- 1.1.1.298
- acetyl-coa
- aurantiacus
- carboxylase
- chloroflexus
-
autotrophic
- metallosphaera
-
3-hydroxypropionate/4-hydroxybutyrate
- sedula
-
malonyl-coenzyme
-
acetyl-coenzyme
- succinyl-coa
- propionyl-coa
-
acrylic
-
value-added
- synthesis
-
transhydrogenase
- sulfolobales
-
reductase-dependent
- crenarchaeota
The enzyme appears in viruses and cellular organisms
Synonyms
malonyl-coa reductase, malonic semialdehyde reductase, malonate semialdehyde reductase, bi-functional malonyl-coa reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-HIBADH
3-hydroxyisobutyrate dehydrogenase
bi-functional malonyl-CoA reductase
malonate semialdehyde reductase
malonic semialdehyde reductase
malonyl-CoA reductase
MCR
MSAR
Msed_1993
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
150386-09-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
-
?
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+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
the bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75. The C-terminal subdomain MCR-C reduces malonyl-CoA to malonate semialdehyde, while the N-terminal subdomain MCR-N reduces malonate semialdehyde to 3-HP
-
-
-
additional information
?
-
-
the bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75. The C-terminal subdomain MCR-C reduces malonyl-CoA to malonate semialdehyde, while the N-terminal subdomain MCR-N reduces malonate semialdehyde to 3-HP
-
-
-
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
-
-
?
additional information
?
-
the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview
-
-
-
additional information
?
-
-
the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview
-
-
-
additional information
?
-
the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview
-
-
-
additional information
?
-
succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
-
-
?
additional information
?
-
-
succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
-
-
?
additional information
?
-
succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
-
-
-
r
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
-
-
-
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
-
-
?
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
-
-
?
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+
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+
-
-
-
?
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
-
-
?
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
?
-
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
the NADPH cofactor bound in MCR N-terminal domain is stabilized by hydrogen bonds with the side chains of Arg55, Arg59, Asp84, Asn151, Tyr744 and Lys195, and the main chains of Asn34, Leu35, Gly85, Asn111, Gly113 and Ile224, and by interaction with C-terminal resdiues by hydrogen bonds with the side chains of Ser88, Arg611, Arg612, Asp646, Tyr744 and Lys748, and the main chains of Ser588, Ala589, Ile591, Arg611, Arg612, Val647, Asn673 and Val776, cofactor binding site structure, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
-
up to 0.2 mM, no effect on activity: MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4
additional information
-
no metal ion requirement, no effects by 0.2 mM 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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibitory: EDTA and ethylene glykol, up to 0.2 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetic analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 45
37 - 60
63% of maximal activity at 60°C, maximal activity at 50°C, about 30% at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme
UniProt
brenda
bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the enzyme is most active in autotrophically grown Chloroflexus aurantiacus at 57°C
brenda
low activity in heterotrophically-grown cell
brenda
-
low activity in heterotrophically-grown cell
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview
evolution
-
distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview
-
metabolism
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
metabolism
3-hydroxypropionic acid (3HP) production via MCR dependent pathway, overview. The bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75
metabolism
enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview
metabolism
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from acetate via malonyl-CoA in the malonyl-CoA reductase pathway, enzyme MCR shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview
metabolism
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from malonyl-CoA via the malonyl-CoA reductase pathway, it shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview
metabolism
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from malonyl-CoA via the malonyl-CoA reductase pathway, it shows malonyl-CoA reductase activity and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid. 3HP can be produced from several intermediates, such as glycerol, malonyl-CoA, and beta-alanine. Among all these biosynthetic routes, the malonyl-CoA pathway has some distinct advantages, including a broad feedstock spectrum, thermodynamic feasibility, and redox neutrality. Comparison of the different metabolic routes for 3HP biosynthesis from glycerol or glucose, overview
metabolism
-
the enzyme from Escherichia coli synthesizes 3-hydroxypropionate (3-HP) from malonate semialdehyde via the beta-alanine pathway, overview. The transformation of beta-alanine to malonic semialdehyde relies on GABT (gamma-aminobutyrate transaminase) and BAPAT (beta-alanine-pyruvate aminotransferase)
metabolism
-
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
-
metabolism
-
enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview
-
physiological function
-
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