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Literature summary extracted from

  • Liu, C.; Ding, Y.; Xian, M.; Liu, M.; Liu, H.; Ma, Q.; Zhao, G.
    Malonyl-CoA pathway a promising route for 3-hydroxypropionate biosynthesis (2017), Crit. Rev. Biotechnol., 37, 933-941 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.298 synthesis the enzyme is very useful for 3-hydroxypropionate biosynthesis and production Chloroflexus aurantiacus
1.2.1.75 synthesis the enzyme is very useful for 3-hydroxypropionate biosynthesis and production Chloroflexus aurantiacus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.298 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 Chloroflexus aurantiacus
1.2.1.75 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.298 malonate semialdehyde + NADPH + H+ Chloroflexus aurantiacus
-
 3-hydroxypropanoate + NADP+
-
 ?
1.2.1.75 malonyl-CoA + NADPH + H+ Chloroflexus aurantiacus
-
 malonate semialdehyde + CoA + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.298 Chloroflexus aurantiacus Q6QQP7 bifunctional enzyme
-
1.2.1.75 Chloroflexus aurantiacus Q6QQP7 bifunctional enzyme
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.298 additional information the enzyme is most active in autotrophically grown Chloroflexus aurantiacus at 57°C Chloroflexus aurantiacus
-
1.2.1.75 additional information the enzyme is most active in autotrophically grown Chloroflexus aurantiacus at 57°C Chloroflexus aurantiacus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.298 malonate semialdehyde + NADPH + H+
-
 Chloroflexus aurantiacus 3-hydroxypropanoate + NADP+
-
 ?
1.2.1.75 malonyl-CoA + NADPH + H+
-
 Chloroflexus aurantiacus malonate semialdehyde + CoA + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.298 malonyl-CoA reductase UniProt Chloroflexus aurantiacus
1.1.1.298 MCR
-
 Chloroflexus aurantiacus
1.1.1.298 More see also EC 1.2.1.75 Chloroflexus aurantiacus
1.2.1.75 malonyl-CoA reductase UniProt Chloroflexus aurantiacus
1.2.1.75 MCR
-
 Chloroflexus aurantiacus
1.2.1.75 More see also EC 1.1.1.298 Chloroflexus aurantiacus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.298 NADPH
-
 Chloroflexus aurantiacus
1.2.1.75 NADPH
-
 Chloroflexus aurantiacus

General Information

EC Number General Information Comment Organism
1.1.1.298 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 Chloroflexus aurantiacus
1.1.1.298 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 Chloroflexus aurantiacus
1.2.1.75 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
1.2.1.75 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