EC Number   |
General Information |
Reference |
|---|
    1.1.1.298 | evolution |
distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview |
-, 762978 |
| 1.1.1.298 | metabolism |
3-hydroxypropionic acid (3HP) production via MCR dependent pathway, overview. The bifunctional enzyme shows malonate semialdehyde reduction activity and also malonyl-CoA reduction activity, EC 1.2.1.75 |
763426 |
| 1.1.1.298 | metabolism |
enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview |
-, 762978 |
| 1.1.1.298 | metabolism |
the bifunctional enzyme from Chloroflexus aurantiacus synthesizes 3-hydroxypropionate (3-HP) from acetate via malonyl-CoA in the malonyl-CoA reductase pathway, enzyme MCR 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 |
762883 |
| 1.1.1.298 | 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 |
763082 |
| 1.1.1.298 | 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. 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 |
762940 |
| 1.1.1.298 | 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) |
763082 |
| 1.1.1.298 | metabolism |
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea |
-, 698628 |
| 1.1.1.298 | more |
Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR) |
-, 762978 |
| 1.1.1.298 | physiological function |
enzyme is part of an autotrophic 3-hydroxypropionate/4-hydroxybutyrate carbon dioxide assimilation pathway in Metallospaera sedula. In the pathway, CO2 is fixed with acetyl-CoA/propionyl-CoA carboxylase as key carboxylating enzyme. One acetyl-CoA and two bicarbonate molecules are reductively converted via 3-hydroxypropionate to succinyl-CoA |
701222 |
