EC Number   |
General Information |
Reference |
|---|
   1.2.1.75 | evolution |
distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview |
-, 762978 |
| 1.2.1.75 | metabolism |
3-hydroxypropionic acid (3HP) production via MCR dependent pathway, overview. The bifunctional enzyme shows malonate semialdehyde reduction activity, EC 1.1.1.298, and also malonyl-CoA reduction activity |
763426 |
| 1.2.1.75 | metabolism |
enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview |
-, 762978 |
| 1.2.1.75 | 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, EC 1.1.1.298, and converts malonyl-CoA to malonate semialdehyde and CoA using NADPH. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, overview |
762883 |
| 1.2.1.75 | 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. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, EC 1.1.1.298, overview |
763082 |
| 1.2.1.75 | 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. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, EC 1.1.1.298. 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 |
| 1.2.1.75 | metabolism |
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea |
698628 |
| 1.2.1.75 | more |
Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR) |
762978 |
| 1.2.1.75 | 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. The malonate semialdehyde is then reduced to 3-hydroxypropionic acid, EC 1.1.1.298, overview |
762940, 763082 |
| 1.2.1.75 | physiological function |
the N-terminal region of MCR (MCR-N, amino acids 1-549) and the C-terminal region of MCR (MCR-C, amino acids 550-1219) are functionally distinct. Malonyl-CoA is reduced into free intermediate malonate semialdehyde with NADPH by the MCR-C fragment, and further reduced to 3-hydroxypropionate by the MCR-N fragment, the initial reduction of malonyl-CoA being rate limiting. The TGXXXG(A)X(1-2)G and YXXXK motifs are important for enzyme activities of both MCR-N and MCR-C fragments, and the enzyme activity increases when MCR is separated into two individual fragments. The MCR-C fragment has higher affinity for malonyl-CoA and 4-times higher Kcat/Km value than MCR |
741279 |
