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Literature summary for 1.1.1.298 extracted from

  • Ji, R.Y.; Ding, Y.; Shi, T.Q.; Lin, L.; Huang, H.; Gao, Z.; Ji, X.J.
    Metabolic engineering of yeast for the production of 3-hydroxypropionic acid (2018), Front. Microbiol., 9, 2185 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.298

Application

Application Comment Organism
synthesis developments in 3-hydroxypropionate (HP) production involving the enzyme using Saccharomyces cerevisiae as an industrial host. By combining genome-scale engineering tools, malonyl-CoA biosensors and optimization of downstream fermentation, the production of 3-HP in yeast has the potential to reach or even exceed the yield of chemical production Escherichia coli
synthesis developments in 3-hydroxypropionate (HP) production involving the enzyme using Saccharomyces cerevisiae as an industrial host. By combining genome-scale engineering tools, malonyl-CoA biosensors and optimization of downstream fermentation, the production of 3-HP in yeast has the potential to reach or even exceed the yield of chemical production Chloroflexus aurantiacus

Protein Variants

Protein Variants Comment Organism
additional information the beta-alanine pathway involving the enzyme is successfully constructed in Saccharomyces cerevisiae, developments in 3-hydroxypropionate production using yeast as an industrial host, method, overview Escherichia coli
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 Chloroflexus aurantiacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
malonate semialdehyde + NADPH + H+ Escherichia coli
-
 3-hydroxypropanoate + NADP+
-
 ?
malonate semialdehyde + NADPH + H+ Chloroflexus aurantiacus
-
 3-hydroxypropanoate + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Chloroflexus aurantiacus Q6QQP7 bifunctional enzyme
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonate semialdehyde + NADPH + H+
-
 Escherichia coli 3-hydroxypropanoate + NADP+
-
 ?
malonate semialdehyde + NADPH + H+
-
 Chloroflexus aurantiacus 3-hydroxypropanoate + NADP+
-
 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Escherichia coli
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, cf. EC 1.2.1.75. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview Chloroflexus aurantiacus
metabolism the enzyme from Escherichia coli synthesizes 3-hydroxypropionate (3-HP) from malonate semialdehyde via the beta-alanine pathway, overview. The transformation of beta-alanine to malonic semialdehyde relies on GABT (gamma-aminobutyrate transaminase) and BAPAT (beta-alanine-pyruvate aminotransferase) Escherichia coli
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