EC Number |
Protein Variants |
Reference |
---|
1.2.1.75 | more |
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 |
-, 722819 |
1.2.1.75 | 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 |
-, 740950 |
1.2.1.75 | N940V/K1106W/S1114R |
the mutations increase the activity of C-terminal of the enzyme by 5.54fold as compared to the wild type |
762880 |
1.2.1.75 | more |
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 |
762883 |
1.2.1.75 | N940V/K1106W/S1114R |
site-directed mutagenesis, the mutant shows increased enzyme activity compared to wild-type enzyme |
762883 |
1.2.1.75 | more |
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 |
762940 |
1.2.1.75 | I798A |
the mutant of the C-terminal domain shows less than 30% activity as compared to the wild type enzyme |
762978 |
1.2.1.75 | K195A |
the mutant of the N-terminal domain is almost completely inactive as compared to the wild type enzyme |
762978 |
1.2.1.75 | K748A |
the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme |
762978 |
1.2.1.75 | K802A |
the mutant of the C-terminal domain shows about 95% activity as compared to the wild type enzyme |
762978 |