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Literature summary extracted from

  • Liang, B.; Sun, G.; Wang, Z.; Xiao, J.; Yang, J.
    Production of 3-hydroxypropionate using a novel malonyl-CoA-mediated biosynthetic pathway in genetically engineered E. coli strain (2019), Green Chem., 21, 6103-6115 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.298 gene mcr, recombinant expression of MCR enzyme mutant in Escherichia coli strain CE43(DE3), coexpression with malonyl-CoA synthetase (MatB) from Rhodopseudomonas palustris, native transhydrogenase (PntAB), and NAD kinase (YfjB) Chloroflexus aurantiacus
1.2.1.75 expressed in Escherichia coli C43 (DE3) cells Chloroflexus aurantiacus
1.2.1.75 gene mcr, recombinant expression of MCR enzyme mutant in Escherichia coli strain CE43(DE3), coexpression with malonyl-CoA synthetase (MatB) from Rhodopseudomonas palustris, native transhydrogenase (PntAB), and NAD kinase (YfjB) Chloroflexus aurantiacus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.298 additional information production of 3-hydroxypropionate using a novel malonyl-CoA-mediated biosynthetic pathway in genetically engineered Escherichia coli strain. Heterologously coexpressing the mutant of malonyl-CoA reductase (MCR) from Chloroflexus aurantiacus and malonyl-CoA synthetase (MatB) from Rhodopseudomonas palustris in the Escherichia coli C43 (DE3) strain. To further enhance the production of 3-HP, native transhydrogenase (PntAB) and NAD kinase (YfjB) genes are expressed to increase the NADPH supply in Escherichia coli. The final genetically modified strain SGN78 shows a significant improvement in malonate utilization and produced 1.20 g/l of 3-HP in the flask culture. Identification of suitable malonate transporters in Rhodobacter capsulatus and Sinorhizobium meliloti, and coexpression of transporter MatB in Escherichia coli. The enzyme activity increases when the N-terminal and C-terminal regions of MCR are separated by fusing a flexible linker (GGGGS) between the two enzymatic units. Optimization of fermentation conditions and improvement of NADPH supply increase 3-HP production rate Chloroflexus aurantiacus
1.1.1.298 N940V/K1106W/S1114R site-directed mutagenesis, mutant N940V/K1106W/S1114R improves the catalytic efficiency by 14.2fold over the wild-type Chloroflexus aurantiacus
1.2.1.75 additional information production of 3-hydroxypropionate using a novel malonyl-CoA-mediated biosynthetic pathway in genetically engineered Escherichia coli strain. Heterologously coexpressing the mutant of malonyl-CoA reductase (MCR) from Chloroflexus aurantiacus and malonyl-CoA synthetase (MatB) from Rhodopseudomonas palustris in the Escherichia coli C43 (DE3) strain. To further enhance the production of 3-HP, native transhydrogenase (PntAB) and NAD kinase (YfjB) genes are expressed to increase the NADPH supply in Escherichia coli. The final genetically modified strain SGN78 shows a significant improvement in malonate utilization and produced 1.20 g/l of 3-HP in the flask culture. Identification of suitable malonate transporters in Rhodobacter capsulatus and Sinorhizobium meliloti, and coexpression of transporter MatB in Escherichia coli. The enzyme activity increases when the N-terminal and C-terminal regions of MCR are separated by fusing a flexible linker (GGGGS) between the two enzymatic units. Optimization of fermentation conditions and improvement of NADPH supply increase 3-HP production rate Chloroflexus aurantiacus
1.2.1.75 N940V/K1106W/S1114R site-directed mutagenesis, mutant N940V/K1106W/S1114R improves the catalytic efficiency by 14.2fold over the wild-type Chloroflexus aurantiacus
1.2.1.75 N940V/K1106W/S1114R the mutations improve the catalytic efficiency by 14.2fold over the wild type 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 malonate semialdehyde + NADPH + H+ Chloroflexus aurantiacus
-
 3-hydroxypropionic acid + 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
-
-
1.2.1.75 Chloroflexus aurantiacus Q6QQP7 bifunctional enzyme
-

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 malonate semialdehyde + NADPH + H+
-
 Chloroflexus aurantiacus 3-hydroxypropionic acid + NADP+
-
 ?
1.2.1.75 malonyl-CoA + NADPH + H+
-
 Chloroflexus aurantiacus malonate semialdehyde + CoA + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.298 homodimer
-
 Chloroflexus aurantiacus
1.2.1.75 ? x * 132000, SDS-PAGE Chloroflexus aurantiacus
1.2.1.75 homodimer
-
 Chloroflexus aurantiacus

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
-
 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