1.2.1.75: malonyl-CoA reductase (malonate semialdehyde-forming)
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For detailed information about malonyl-CoA reductase (malonate semialdehyde-forming), go to the full flat file.
Reaction
Synonyms
bi-functional malonyl-CoA reductase, malonate semialdehyde reductase, malonate-semialdehyde dehydrogenase, malonyl CoA reductase (malonate semialdehyde-forming), malonyl-CoA reductase, MCR, More, MSAR
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1.2.1.75 malonyl-CoA reductase (malonate semialdehyde-forming)Advanced search results
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results (Engineering
Engineering on EC 1.2.1.75 - malonyl-CoA reductase (malonate semialdehyde-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N940V/K1106W/S1114R
I798A
the mutant of the C-terminal domain shows less than 30% activity as compared to the wild type enzyme
K195A
the mutant of the N-terminal domain is almost completely inactive as compared to the wild type enzyme
K748A
the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme
K802A
the mutant of the C-terminal domain shows about 95% activity as compared to the wild type enzyme
K926A
the mutant of the C-terminal domain shows about 90% activity as compared to the wild type enzyme
M662A
the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme
N740A
the mutant of the C-terminal domain shows about 15% activity as compared to the wild type enzyme
N805A
the mutant of the C-terminal domain shows less than 60% activity as compared to the wild type enzyme
R1166A
the mutant of the C-terminal domain shows less than 20% activity as compared to the wild type enzyme
R188A
the mutant of the N-terminal domain shows less than 10% activity as compared to the wild type enzyme
R741A
the mutant of the C-terminal domain shows less than 5% activity as compared to the wild type enzyme
R780A
the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme
R794A
the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme
S726A
the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme
T178A
the mutant of the N-terminal domain is almost completely inactive as compared to the wild type enzyme
Y185A
the mutant of the N-terminal domain shows less than 20% activity as compared to the wild type enzyme
Y191A
the mutant of the N-terminal domain shows less than 10% activity as compared to the wild type enzyme
Y738A
the mutant of the C-terminal domain shows about 10% activity as compared to the wild type enzyme
Y744A
the mutant of the C-terminal domain shows less than 5% activity as compared to the wild type enzyme
synthesis
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
N940V/K1106W/S1114R
the mutations improve the catalytic efficiency by 14.2fold over the wild type
N940V/K1106W/S1114R
the mutations increase the activity of C-terminal of the enzyme by 5.54fold as compared to the wild type
synthesis
heterologous expression of the malonyl-CoA dependent pathway genes malonyl-CoA reductase and malonate semialdehyde reductase enables Synechococcus elongatus to synthesize 3-hydroxypropionic acid to a final titer of 665 mg/l
synthesis
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heterologous expression of the malonyl-CoA dependent pathway genes malonyl-CoA reductase and malonate semialdehyde reductase enables Synechococcus elongatus to synthesize 3-hydroxypropionic acid to a final titer of 665 mg/l
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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, malonate semialdehyde is then reduced to 3-hydroxypropionic acid (EC 1.1.1.298). 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%
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
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
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
additional information
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the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
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