Literature summary for 1.2.1.75 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 .

Search for more literature for 1.2.1.75

Application

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

Protein Variants

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/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Chloroflexus aurantiacus	Q6QQP7	bifunctional enzyme	-

Source Tissue

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
malonyl-CoA + NADPH + H+	-	Chloroflexus aurantiacus	malonate semialdehyde + CoA + NADP+	-	?

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Chloroflexus aurantiacus

General Information

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

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Release 2023.1 (January 2023)