Crystallization (Comment) | Organism |
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crystallization trials of the full-length MCR fail, thus production of the N-terminal domain (MCRND, Met1-Pro567) and the C-terminal domain (MCRCD, Gly568-Val1230) separately, X-ray diffraction structure determination and analysis at resolutions of 2.20 and 1.80 A, respectively, by a single-wavelength anomalous dispersion (SAD) method | Erythrobacter dokdonensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonate semialdehyde + NADPH + H+ | Erythrobacter dokdonensis | - |
3-hydroxypropanoate + NADP+ | - |
? | |
malonate semialdehyde + NADPH + H+ | Erythrobacter dokdonensis DSW-74 | - |
3-hydroxypropanoate + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Erythrobacter dokdonensis | A0A1A7BFR5 | Porphyrobacter dokdonensis | - |
Erythrobacter dokdonensis DSW-74 | A0A1A7BFR5 | Porphyrobacter dokdonensis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonate semialdehyde + NADPH + H+ | - |
Erythrobacter dokdonensis | 3-hydroxypropanoate + NADP+ | - |
? | |
malonate semialdehyde + NADPH + H+ | - |
Erythrobacter dokdonensis DSW-74 | 3-hydroxypropanoate + NADP+ | - |
? | |
additional information | the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview | Erythrobacter dokdonensis | ? | - |
- |
|
additional information | the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview | Erythrobacter dokdonensis DSW-74 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
homodimer | subunit structures and interaction analysis | Erythrobacter dokdonensis |
More | olecular architecture of the full-length MCR, modeling, overview | Erythrobacter dokdonensis |
Synonyms | Comment | Organism |
---|---|---|
bi-functional malonyl-CoA reductase | - |
Erythrobacter dokdonensis |
malonate semialdehyde reductase | - |
Erythrobacter dokdonensis |
MCR | - |
Erythrobacter dokdonensis |
More | see also EC 1.2.1.75 | Erythrobacter dokdonensis |
MSAR | - |
Erythrobacter dokdonensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | the NADPH cofactor bound in MCR N-terminal domain is stabilized by hydrogen bonds with the side chains of Arg55, Arg59, Asp84, Asn151, Tyr744 and Lys195, and the main chains of Asn34, Leu35, Gly85, Asn111, Gly113 and Ile224, and by interaction with C-terminal resdiues by hydrogen bonds with the side chains of Ser88, Arg611, Arg612, Asp646, Tyr744 and Lys748, and the main chains of Ser588, Ala589, Ile591, Arg611, Arg612, Val647, Asn673 and Val776, cofactor binding site structure, overview | Erythrobacter dokdonensis |
General Information | Comment | Organism |
---|---|---|
evolution | distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview | Erythrobacter dokdonensis |
metabolism | enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview | Erythrobacter dokdonensis |
additional information | Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR) | Erythrobacter dokdonensis |