Cloned (Comment) | Organism |
---|---|
gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3) | Pseudomonas sp. |
Crystallization (Comment) | Organism |
---|---|
purified recombinant His-tagged enzyme, microseeding, mixing of 150 nl of 5 mg/ml protein in 40 mM Tris Cl, 150 mM NaCl, 2 mM KCl, and TBS, pH 8, with 150 nl of reservoir solution containing 23.7% w/v PEG 3350, 0.208 M trisodium citrate, 0.1 M Bis-Tris propane, pH 7.55, and equilibration against 0.05 ml of reservoir solution, at 8°C, X-ray diffraction structure determination and analysis at 2.95 A resolution, molecular replacement and modeling using PDB entry 4zz7 as a template | Pseudomonas sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-oxopropanoate + CoA + NAD+ | Pseudomonas sp. | - |
acetyl-CoA + CO2 + NADH | - |
? | |
3-oxopropanoate + CoA + NAD+ | Pseudomonas sp. AAC | - |
acetyl-CoA + CO2 + NADH | - |
? | |
additional information | Pseudomonas sp. | the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed | ? | - |
? | |
additional information | Pseudomonas sp. AAC | the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas sp. | - |
- |
- |
Pseudomonas sp. AAC | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration to over 95% purity | Pseudomonas sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-oxopropanoate + CoA + NAD+ | - |
Pseudomonas sp. | acetyl-CoA + CO2 + NADH | - |
? | |
3-oxopropanoate + CoA + NAD+ | - |
Pseudomonas sp. AAC | acetyl-CoA + CO2 + NADH | - |
? | |
additional information | the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed | Pseudomonas sp. | ? | - |
? | |
additional information | the malonate-semialdehyde dehydrogenase is selective towards malonate semialdehyde and generates acetyl-CoA in an NAD-dependent and CoA-dependent reaction, although a slower CoA-independent reaction generating acetate is also observed | Pseudomonas sp. AAC | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | the monomeric structure is made up of two primary domains. Each has a central extended beta-sheet surrounded by alpha-helices, with a cleft between them which holds the cofactor. The second primary domain extends from residues 249 to 444 and has a central beta-sheet of seven strands surrounded by alpha-helices. This second beta-sheet is extended by the three beta-strands of the neighbouring dimer extension (residues 119-136 and 444-494) to make a beta-sheet of ten strands in the dimer structure. The finger extension (residues 119-136 and 444-480) forms a three-stranded beta-sheet extension which pulls the dimer structure together, but is also used as a hook to pull in a neighbouring dimer and form the basis of the hexameric structure | Pseudomonas sp. |
Synonyms | Comment | Organism |
---|---|---|
FG99_15390 | - |
Pseudomonas sp. |
KES23460 | - |
Pseudomonas sp. |
malonate-semialdehyde dehydrogenase | - |
Pseudomonas sp. |
methylmalonate-semialdehyde dehydrogenase | UniProt | Pseudomonas sp. |
NAD-dependent malonate-semialdehyde dehydrogenase | - |
Pseudomonas sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | the central beta-sheet of five strands surrounded by alpha-helices in the first domain forming the cofactor-binding site, including residues 39-248, minus the extension of residues 119-136 | Pseudomonas sp. |