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Literature summary extracted from

  • Luo, H.; Zhou, D.; Liu, X.; Nie, Z.; Quiroga-Sanchez, D.; Chang, Y.
    Production of 3-hydroxypropionic acid via the propionyl-CoA pathway using recombinant Escherichia coli strains (2016), PLoS ONE, 11, e0156286 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.116 gene hpcd, coexpression of 3-hydroxypropionyl-CoA dehydratase (HPCD) with propionyl-CoA dehydrogenase (PACD) encoded by gene pacd from Candida rugosa and propionate CoA-transferase (PCT) encoded by gene pct from Megasphaera elsdenii in Escherichia coli strain BL21(DE3) under control of the T7 promoter Chloroflexus aurantiacus

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.116 additional information production of the commercially promising platform chemical 3-hydroxypropionic acid (3-HP) via the propionyl-CoA pathway in genetically engineered Escherichia coli strain BL21(DE3). Propionate CoA-transferase from Megasphaera elsdenii and 3-hydroxypropionyl-CoA dehydratase (HPCD) from Chloroflexus aurantiacus are expressed along with propionyl-CoA dehydrogenase (PACD) from Candida rugosa, the 3-hydroxypropanoate titer of the resulting Escherichia coli Ec-PPH strain is improved by 6fold. When cultured at 30°C with 1% glucose in addition to propionate, 3-hydroxypropanoate production by Ec-PPH increases 2fold and 12fold compared to the cultivation at 37°C (4.23 mM) or without glucose (0.68 mM), respectively. Deletion of the ygfH gene encoding propionyl-CoA: succinate CoA-transferase from Ec-PPH (resulting in the strain Ec-DELTAY-PPH) leads to increase of 3-hydroxypropanoate production in shake flask experiments (15.04 mM), whereas the strain Ec-DELTAY-PPH with deletion of the prpC gene (encoding methylcitrate synthase in the methylcitrate cycle) produces 17.76 mM of 3-HP. The strain Ec-DELTAY-DELTAP-PPH with both ygfH and prpC genes deleted produces 24.14 mM of 3-HP, thus showing an 18fold increase in the 3-hydroxypropanoate titer in compare to the strain Ec-P. Disruption of the competing metabolic pathways. Established transgenic metabolic pathway, method, overview Chloroflexus aurantiacus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.116 3-hydroxypropanoyl-CoA Chloroflexus aurantiacus
-
acryloyl-CoA + H2O
-
r
6.2.1.17 ATP + propanoate + CoA Escherichia coli
-
AMP + diphosphate + propanoyl-CoA
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.116 Chloroflexus aurantiacus
-
-
-
6.2.1.17 Escherichia coli P77495
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.116 3-hydroxypropanoyl-CoA
-
Chloroflexus aurantiacus acryloyl-CoA + H2O
-
r
6.2.1.17 ATP + propanoate + CoA
-
Escherichia coli AMP + diphosphate + propanoyl-CoA
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.116 3-hydroxypropionyl-CoA dehydratase
-
Chloroflexus aurantiacus
4.2.1.116 HPCD
-
Chloroflexus aurantiacus
6.2.1.17 Propionyl-CoA synthetase
-
Escherichia coli
6.2.1.17 PrpE
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.116 30
-
in vivo Chloroflexus aurantiacus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.1.116 30 37 recombinant PACD activity in vivo is the highest at 30°C, it decreased to 30% activity when incubated for 2 h at 37°C Chloroflexus aurantiacus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.116 30 37 recombinant PACD activity in vivo is the highest at 30°C, it decreased to 30% activity when incubated for 2 h at 37°C Chloroflexus aurantiacus

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.17 ATP
-
Escherichia coli

General Information

EC Number General Information Comment Organism
4.2.1.116 metabolism propionyl-CoA is a key precursor for 3-hydroxypropanoate formation Chloroflexus aurantiacus