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Literature summary for 1.2.1.75 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)

Cloned (Comment) Organism
expressed in Escherichia coli C43 (DE3) cells Chloroflexus aurantiacus
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

Protein Variants Comment Organism
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
N940V/K1106W/S1114R site-directed mutagenesis, mutant N940V/K1106W/S1114R improves the catalytic efficiency by 14.2fold over the wild-type Chloroflexus aurantiacus
N940V/K1106W/S1114R the mutations improve the catalytic efficiency by 14.2fold over the wild type Chloroflexus aurantiacus

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonate semialdehyde + NADPH + H+
-
Chloroflexus aurantiacus 3-hydroxypropionic acid + NADP+
-
?
malonyl-CoA + NADPH + H+
-
Chloroflexus aurantiacus malonate semialdehyde + CoA + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 132000, SDS-PAGE Chloroflexus aurantiacus
homodimer
-
Chloroflexus aurantiacus

Synonyms

Synonyms Comment Organism
malonyl-CoA reductase
-
Chloroflexus aurantiacus
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