Any feedback?
No. of entries
Information on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.298
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
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.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 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
showSynonyms
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
MetaCyc
3-hydroxypropanoate cycle, 3-hydroxypropanoate/4-hydroxybutanate cycle, beta-alanine degradation III, glyoxylate assimilation, uracil degradation III
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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanoate + NAD+
malonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NAD+
malonate-semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH
3-hydroxypropionate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
Substrates: -
Products: spectrophotometric product determination
Products: spectrophotometric product determination
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: -
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
Substrates: 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, additionally exhibits 3-hydroxypropionate dehydrogenase activity
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
malonate semialdehyde + NADH + H+
3-hydroxypropanoate + NAD+
Substrates: NADH can partially substitute (20% activity) for NADPH
Products: -
Products: -
?
malonate semialdehyde + NADH + H+
3-hydroxypropanoate + NAD+
Substrates: NADH can partially substitute (20% activity) for NADPH
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: NADH can partially substitute (20% activity) for NADPH
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: NADH can partially substitute (20% activity) for NADPH
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: succinic semialdehyde, acetaldehyde, butyraldehyde, propionaldehyde, or glutaraldehyde do not serve as a substrate
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanoate + NADP+
malonate-semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
malonate-semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropanoate + NADP+
Substrates: the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
Substrates: -
Products: -
Products: -
?
malonate semialdehyde + NADPH + H+
3-hydroxypropionate + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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 kinetic analysis, overview
-
additional information
additional information
-
steady-state kinetics, 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
Highest Expressing Human Cell Lines
Cell Line LinksPlease 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
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 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 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
enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview
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
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 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
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
physiological function
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
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
-
the organism assimilates CO2 by the 3-hydroxypropionate cycle, and malonyl-CoA reductase is an essential enzyme for the cycle
-
additional information
Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR)
additional information
-
Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR)
additional information
-
Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR)
-
Show AA Sequence and Transmembrane Helices (2979 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotrimer
additional information
additional information
olecular architecture of the full-length MCR, modeling, overview
additional information
-
olecular architecture of the full-length MCR, modeling, overview
additional information
-
olecular architecture of the full-length MCR, modeling, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization trials of the full-length MCR fail, thus production of the N-terminal domain (MCRND, Met1-Pro567) and the C-terminal domain (MCRCD, Gly568-Val1230) separately, X-ray diffraction structure determination and analysis at resolutions of 2.20 and 1.80 A, respectively, by a single-wavelength anomalous dispersion (SAD) method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N940V/K1106W/S1114R
additional information
N940V/K1106W/S1114R
site-directed mutagenesis, the mutant shows increased enzyme activity compared to wild-type enzyme
N940V/K1106W/S1114R
site-directed mutagenesis, mutant N940V/K1106W/S1114R improves the catalytic efficiency by 14.2fold over the wild-type
additional information
the malonyl-CoA reductase pathway involving the enzyme is successfully constructed in Saccharomyces cerevisiae, developments in 3-hydroxypropionate production using yeast as an industrial host, method, overview. Requirement of improving the supply of the cofactor NADPH due to high expense of NADPH
additional information
3-hydroxypropionate (3HP) is an attractive platform chemical, serving as a precursor to a variety of commodity chemicals like acrylate and acrylamide, as well as a monomer of a biodegradable plastic. It can be used to establish a sustainable way to produce these commercially important chemicals and materials, fermentative production of 3HP is widely investigated in recent years. Reconstruction of the malonyl-CoA pathway in Escherichia coli employing acetyl-CoA carboxylase (ACC) for the conversion of acetyl-CoA into malonyl-CoA, which is converted into 3HP with a two-step reduction catalyzed by malonyl-CoA reductase (MCR) that converts malonyl-CoA to malonate semialdehyde and CoA (EC 1.2.1.75), malonate semialdehyde is then reduced to 3-hydroxypropionic acid. Redirection of carbon flux toward 3HP biosynthesis by metabolic engineering e.g. through manipulation of various regulation factors controlling central carbon metabolism, such as CsrB, SgrS and ArcA, or through inhibition of the activity of 3-oxoacyl-ACP synthase I and II with the antibiotic cerulenin to suppress fatty acids biosynthesis, or through improving catalysis of key enzymes, enhancing cofactor and energy supply, and promoting catalytic efficiency of MCR. Compared to Escherichia coli, Saccharomyces cerevisiae is the better host
additional information
engineering of type II methanotroph Methylosinus trichosporium strain OB3b for 3-hydroxypropionic acid (3HP) production by reconstructing malonyl-CoA pathway through heterologous expression of Chloroflexus aurantiacus malonyl-CoA reductase (MCR), a bifunctional enzyme. Engineering of the supply of malonyl-CoA precursors by overexpressing endogenous acetyl-CoA carboxylase (ACC), substantially enhancing the production of 3HP. Overexpression of biotin protein ligase (BPL) and malic enzyme (NADP+-ME) leads to 22.7% and 34.5% increase, respectively, in 3HP titer in ACC-overexpressing cells. Also, the acetyl-CoA carboxylation bypass route is reconstructed to improve 3HP productivity. Coexpression of methylmalonyl-CoA carboxyltransferase (MMC) of Propionibacterium freudenreichii and phosphoenolpyruvate carboxylase (PEPC), which provides the MMC precursor, further improves the 3HP titer. The highest 3HP production of 49 mg/l in the OB3b-MCRMP strain overexpressing MCR, MMC and PEPC results in a 2.4fold improvement of titer compared with that in the only MCR-overexpressing strain. 60.59 mg/l of 3HP are obatined in 42 h using the OB3b-MCRMP strain through bioreactor operation, with a 6.36fold increase of volumetric productivity compared than that in the flask cultures
additional information
-
engineering of type II methanotroph Methylosinus trichosporium strain OB3b for 3-hydroxypropionic acid (3HP) production by reconstructing malonyl-CoA pathway through heterologous expression of Chloroflexus aurantiacus malonyl-CoA reductase (MCR), a bifunctional enzyme. Engineering of the supply of malonyl-CoA precursors by overexpressing endogenous acetyl-CoA carboxylase (ACC), substantially enhancing the production of 3HP. Overexpression of biotin protein ligase (BPL) and malic enzyme (NADP+-ME) leads to 22.7% and 34.5% increase, respectively, in 3HP titer in ACC-overexpressing cells. Also, the acetyl-CoA carboxylation bypass route is reconstructed to improve 3HP productivity. Coexpression of methylmalonyl-CoA carboxyltransferase (MMC) of Propionibacterium freudenreichii and phosphoenolpyruvate carboxylase (PEPC), which provides the MMC precursor, further improves the 3HP titer. The highest 3HP production of 49 mg/l in the OB3b-MCRMP strain overexpressing MCR, MMC and PEPC results in a 2.4fold improvement of titer compared with that in the only MCR-overexpressing strain. 60.59 mg/l of 3HP are obatined in 42 h using the OB3b-MCRMP strain through bioreactor operation, with a 6.36fold increase of volumetric productivity compared than that in the flask cultures
additional information
for the efficient conversion of acetate to 3-hydroxypropionate(3-HP), heterologous mcr (encoding malonyl-CoA reductase) mutant N940V/K1106W/S1114R from Chloroflexus aurantiacus is initially introduced into Escherichia coli. Then, the acetate assimilating pathway and glyoxylate shunt pathway are activated by overexpressing acs (encoding acetyl-CoA synthetase) and deleting iclR (encoding the glyoxylate shunt pathway repressor). Because a key precursor malonyl-CoA is also consumed for fatty acid synthesis, carbon flux to fatty acid synthesis is inhibited by adding cerulenin, which dramatically improves 3-HP production. Method evaluation and optimization, overview
additional information
production of 3-hydroxypropionate using a novel malonyl-CoA-mediated biosynthetic pathway in genetically engineered Escherichia coli strain. Heterologously coexpressing the mutant of malonyl-CoA reductase (MCR) from Chloroflexus aurantiacus and malonyl-CoA synthetase (MatB) from Rhodopseudomonas palustris in the Escherichia coli C43 (DE3) strain. To further enhance the production of 3-HP, native transhydrogenase (PntAB) and NAD kinase (YfjB) genes are expressed to increase the NADPH supply in Escherichia coli. The final genetically modified strain SGN78 shows a significant improvement in malonate utilization and produced 1.20 g/l of 3-HP in the flask culture. Identification of suitable malonate transporters in Rhodobacter capsulatus and Sinorhizobium meliloti, and coexpression of transporter MatB in Escherichia coli. The enzyme activity increases when the N-terminal and C-terminal regions of MCR are separated by fusing a flexible linker (GGGGS) between the two enzymatic units. Optimization of fermentation conditions and improvement of NADPH supply increase 3-HP production rate
additional information
enhancing 3-hydroxypropionic acid production in combination with sugar supply engineering by cell surface-display and metabolic engineering of Schizosaccharomyces pombe. 3-HP production from glucose and cellobiose via the malonyl-CoA pathway, the mcr gene, encoding the bifunctional malonyl-CoA reductase of Chloroflexus aurantiacus, is dissected into two functionally distinct fragments, and the activities of the encoded protein are balanced. The MCR-C fragment reduces malonyl-CoA to malonate semialdehyde, while the MCR-N fragment reduces malonate semialdehyde to 3-HP. To increase the cellular supply of malonyl-CoA and acetyl-CoA, genes encoding endogenous aldehyde dehydrogenase, acetyl-CoA synthase from Salmonella enterica, and endogenous pantothenate kinase are introduced. The resulting strain produces 3-HP at 1.0 g/l from a culture starting at a glucose concentration of 50 g/l. We also engineered the sugar supply by displaying beta-glucosidase (BGL) on the yeast cell surface. When grown on 50 g/l cellobiose, the beta-glucosidase-displaying strain consumes cellobiose efficiently and produces 3-HP at 3.5 g/l. Under fed-batch conditions starting from cellobiose, this strain produces 3-HP at up to 11.4 g/l, corresponding to a yield of 11.2%
additional information
-
enhancing 3-hydroxypropionic acid production in combination with sugar supply engineering by cell surface-display and metabolic engineering of Schizosaccharomyces pombe. 3-HP production from glucose and cellobiose via the malonyl-CoA pathway, the mcr gene, encoding the bifunctional malonyl-CoA reductase of Chloroflexus aurantiacus, is dissected into two functionally distinct fragments, and the activities of the encoded protein are balanced. The MCR-C fragment reduces malonyl-CoA to malonate semialdehyde, while the MCR-N fragment reduces malonate semialdehyde to 3-HP. To increase the cellular supply of malonyl-CoA and acetyl-CoA, genes encoding endogenous aldehyde dehydrogenase, acetyl-CoA synthase from Salmonella enterica, and endogenous pantothenate kinase are introduced. The resulting strain produces 3-HP at 1.0 g/l from a culture starting at a glucose concentration of 50 g/l. We also engineered the sugar supply by displaying beta-glucosidase (BGL) on the yeast cell surface. When grown on 50 g/l cellobiose, the beta-glucosidase-displaying strain consumes cellobiose efficiently and produces 3-HP at 3.5 g/l. Under fed-batch conditions starting from cellobiose, this strain produces 3-HP at up to 11.4 g/l, corresponding to a yield of 11.2%
additional information
-
the beta-alanine pathway involving the enzyme is successfully constructed in Saccharomyces cerevisiae, developments in 3-hydroxypropionate production using yeast as an industrial host, method, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
55
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is oxygen insensitive but sensitive to repeated freezing and thawing
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
gene mcr, recombinant expression in Escherichia coli strain BL21(DE3), coexpression of acetyl-CoA synthetase
gene mcr, recombinant expression of MCR enzyme mutant in Escherichia coli strain CE43(DE3), coexpression with malonyl-CoA synthetase (MatB) from Rhodopseudomonas palustris, native transhydrogenase (PntAB), and NAD kinase (YfjB)
gene mcr, recombinant expression of the Chloroflexus aurantiacus enzyme in Methylosinus trichosporium strain OB3b, subcloning in Escherichia coli strain DH5alpha
gene mcr, separate recombinant expression of the N- and C-terminal subdomains of the enzyme, MCR-C and MCR-N, in Schizosaccharomyces pombe strain FY12804/NBRP, coexpression of acetyl-CoA synthase, gene acsSE, and aldehyde dehydrogenase, gene atd1, under the control of the cam1 promoter
MmsB gene, overexpression in Escherichia coli strain BL21, subcloning in strain DH5alpha
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
developments in 3-hydroxypropionate (HP) production involving the enzyme using Saccharomyces cerevisiae as an industrial host. By combining genome-scale engineering tools, malonyl-CoA biosensors and optimization of downstream fermentation, the production of 3-HP in yeast has the potential to reach or even exceed the yield of chemical production
synthesis
-
developments in 3-hydroxypropionate (HP) production involving the enzyme using Saccharomyces cerevisiae as an industrial host. By combining genome-scale engineering tools, malonyl-CoA biosensors and optimization of downstream fermentation, the production of 3-HP in yeast has the potential to reach or even exceed the yield of chemical production
synthesis
the enzyme is very useful for 3-hydroxypropionate biosynthesis and production
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strauss, G.; Fuchs, G.
Enzymes of a novel autotrophic carbon dioxide fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle
Eur. J. Biochem.
215
633-643
1993
Chloroflexus aurantiacus
brenda
Yao, T.; Xu, L.; Ying, H.; Huang, H.; Yan, M.
The catalytic property of 3-hydroxyisobutyrate dehydrogenase from Bacillus cereus on 3-hydroxypropionate
Appl. Biochem. Biotechnol.
160
694-703
2009
Bacillus cereus, Bacillus cereus ATCC 14579
brenda
Huegler, M.; Menendez, C.; Schaegger, H.; Fuchs, G.
Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO(2) fixation
J. Bacteriol.
184
2404-2410
2002
Chloroflexus aurantiacus
brenda
Kockelkorn, D.; Fuchs, G.
Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: Enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in Sulfolobales
J. Bacteriol.
191
6352-6362
2009
Metallosphaera sedula (A4YI81), Metallosphaera sedula, Metallosphaera sedula DSM 5348 (A4YI81)
brenda
Berg, I.A.; Kockelkorn, D.; Buckel, W.; Fuchs, G.
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea
Science
318
1782-1786
2007
Metallosphaera sedula
brenda
Rathnasingh, C.; Raj, S.M.; Lee, Y.; Catherine, C.; Ashok, S.; Park, S.
Production of 3-hydroxypropionic acid via malonyl-CoA pathway using recombinant Escherichia coli strains
J. Biotechnol.
157
633-640
2012
Chloroflexus aurantiacus (Q6QQP7), Chloroflexus aurantiacus DSM 635 (Q6QQP7)
brenda
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
Thermus thermophilus (Q5SLQ6), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SLQ6)
brenda
Lee, J.; Cha, S.; Kang, C.; Lee, G.; Lim, H.; Jung, G.
Efficient conversion of acetate to 3-hydroxypropionic acid by engineered Escherichia coli
Catalysts
8
525
2018
Chloroflexus aurantiacus (Q6QQP7)
-
brenda
Liu, C.; Ding, Y.; Xian, M.; Liu, M.; Liu, H.; Ma, Q.; Zhao, G.
Malonyl-CoA pathway a promising route for 3-hydroxypropionate biosynthesis
Crit. Rev. Biotechnol.
37
933-941
2017
Chloroflexus aurantiacus (Q6QQP7)
brenda
Son, H.F.; Kim, S.; Seo, H.; Hong, J.; Lee, D.; Jin, K.S.; Park, S.; Kim, K.J.
Structural insight into bi-functional malonyl-CoA reductase
Environ. Microbiol.
22
752-765
2020
Erythrobacter dokdonensis (A0A1A7BFR5), Erythrobacter dokdonensis, Erythrobacter dokdonensis DSW-74 (A0A1A7BFR5)
brenda
Ji, R.Y.; Ding, Y.; Shi, T.Q.; Lin, L.; Huang, H.; Gao, Z.; Ji, X.J.
Metabolic engineering of yeast for the production of 3-hydroxypropionic acid
Front. Microbiol.
9
2185
2018
Chloroflexus aurantiacus (Q6QQP7), Escherichia coli
brenda
Liang, B.; Sun, G.; Wang, Z.; Xiao, J.; Yang, J.
Production of 3-hydroxypropionate using a novel malonyl-CoA-mediated biosynthetic pathway in genetically engineered E. coli strain
Green Chem.
21
6103-6115
2019
Chloroflexus aurantiacus (Q6QQP7)
-
brenda
Nguyen, D.T.N.; Lee, O.K.; Lim, C.; Lee, J.; Na, J.G.; Lee, E.Y.
Metabolic engineering of type II methanotroph, Methylosinus trichosporium OB3b, for production of 3-hydroxypropionic acid from methane via a malonyl-CoA reductase-dependent pathway
Metab. Eng.
59
142-150
2020
Chloroflexus aurantiacus (Q6QQP7), Chloroflexus aurantiacus
brenda
Takayama, S.; Ozaki, A.; Konishi, R.; Otomo, C.; Kishida, M.; Hirata, Y.; Matsumoto, T.; Tanaka, T.; Kondo, A.
Enhancing 3-hydroxypropionic acid production in combination with sugar supply engineering by cell surface-display and metabolic engineering of Schizosaccharomyces pombe
Microb. Cell Fact.
17
176
2018
Chloroflexus aurantiacus (Q6QQP7), Chloroflexus aurantiacus
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.298)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
