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Information on EC 1.1.1.298 - 3-hydroxypropionate dehydrogenase (NADP+)
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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.
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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
3-HIBADH, 3-hydroxyisobutyrate dehydrogenase, 3-hydroxypropionate dehydrogenase, malonate semialdehyde reductase (NADPH), malonic semialdehyde reductase, malonyl-CoA reductase, Msed_1993, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-HIBADH
3-hydroxyisobutyrate dehydrogenase
malonic semialdehyde reductase
Msed_1993
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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
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-
-
?
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
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-
?
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
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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
-
-
?
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
?
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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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-
?
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 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+
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
-
-
?
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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
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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
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INHIBITOR
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 kinetics, overview
-
additional information
additional information
-
steady-state kinetic analysis, 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
37
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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
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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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
low activity in heterotrophically-grown cell
brenda
-
low activity in heterotrophically-grown cell
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
metabolism
evolution
additional information
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 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
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
-
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
-
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
-
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)
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Show AA Sequence and Transmembrane Helices (2506 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
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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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N940V/K1106W/S1114R
additional information
N940V/K1106W/S1114R
-
site-directed mutagenesis, mutant N940V/K1106W/S1114R improves the catalytic efficiency by 14.2fold over the wild-type
N940V/K1106W/S1114R
-
site-directed mutagenesis, the mutant shows increased enzyme activity compared to wild-type enzyme
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
-
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%