Application | Comment | Organism |
---|---|---|
synthesis | the enzyme is very useful for 3-hydroxypropionate biosynthesis and production | Chloroflexus aurantiacus |
Protein Variants | Comment | Organism |
---|---|---|
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 | Chloroflexus aurantiacus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonyl-CoA + NADPH + H+ | Chloroflexus aurantiacus | - |
malonate semialdehyde + CoA + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chloroflexus aurantiacus | Q6QQP7 | bifunctional enzyme | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | the enzyme is most active in autotrophically grown Chloroflexus aurantiacus at 57°C | Chloroflexus aurantiacus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonyl-CoA + NADPH + H+ | - |
Chloroflexus aurantiacus | malonate semialdehyde + CoA + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
malonyl-CoA reductase | UniProt | Chloroflexus aurantiacus |
MCR | - |
Chloroflexus aurantiacus |
More | see also EC 1.1.1.298 | Chloroflexus aurantiacus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Chloroflexus aurantiacus |
General Information | Comment | Organism |
---|---|---|
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. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, EC 1.1.1.298. 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 | Chloroflexus aurantiacus |
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. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, EC 1.1.1.298, overview | Chloroflexus aurantiacus |