EC Number | Application | Comment | Organism |
---|---|---|---|
1.2.1.75 | biotechnology | the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production | Sulfurisphaera tokodaii |
1.2.1.75 | synthesis | MCR is of biotechnological interest for the synthesis of polyester building blocks | Sulfurisphaera tokodaii |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.75 | Escherichia coli Rosetta 2 cells transformed with pTrc99A-Mcr plasmid harbouring mcr gene from Sulfolobus tokodaii | Sulfurisphaera tokodaii |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.2.1.75 | malonyl-CoA reductase in the substrate-free state at 2.05 A resolution and in complex with NADP+ at 1.9 A resolution and in complex with CoA at 2.4 A resolution | Sulfurisphaera tokodaii |
1.2.1.75 | sitting drop method, 18°C | Sulfurisphaera tokodaii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.1.75 | additional information | the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production | Sulfurisphaera tokodaii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.75 | Sulfurisphaera tokodaii | Q96YK1 | - |
- |
1.2.1.75 | Sulfurisphaera tokodaii DSM 16993 | Q96YK1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.75 | - |
Sulfurisphaera tokodaii |
1.2.1.75 | recombinant enzyme purified by heat precipitation at 85°C and concentration by ultrafiltration, gel filtration chromatography using a Superdex 200 HR 26/60 gel filtration column and Resource phenyl chromatography using a Resource phenyl column | Sulfurisphaera tokodaii |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.2.1.75 | malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+ | the protein acts as rigid template to press CoA and NADP into similar S-shaped, superimposable forms | Sulfurisphaera tokodaii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.75 | malonyl-CoA + NADPH + H+ | - |
Sulfurisphaera tokodaii | malonate semialdehyde + CoA + NADP+ | - |
? | |
1.2.1.75 | malonyl-CoA + NADPH + H+ | structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism | Sulfurisphaera tokodaii | malonate semialdehyde + CoA + NADP+ | - |
? | |
1.2.1.75 | malonyl-CoA + NADPH + H+ | - |
Sulfurisphaera tokodaii DSM 16993 | malonate semialdehyde + CoA + NADP+ | - |
? | |
1.2.1.75 | malonyl-CoA + NADPH + H+ | structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism | Sulfurisphaera tokodaii DSM 16993 | malonate semialdehyde + CoA + NADP+ | - |
? | |
1.2.1.75 | succinyl-CoA + NADPH + H+ | - |
Sulfurisphaera tokodaii | succinic semialdehyde + CoA + NADP+ | - |
? | |
1.2.1.75 | succinyl-CoA + NADPH + H+ | - |
Sulfurisphaera tokodaii DSM 16993 | succinic semialdehyde + CoA + NADP+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.1.75 | homotetramer | organized as a dimer of two dimers | Sulfurisphaera tokodaii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.75 | malonyl-CoA reductase | - |
Sulfurisphaera tokodaii |
1.2.1.75 | MCR | - |
Sulfurisphaera tokodaii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.75 | NADPH | - |
Sulfurisphaera tokodaii |