Literature summary for 1.2.1.18 extracted from

Wilding, M.; Scott, C.; Peat, T.S.; Newman, J.
X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC (2017), Acta Crystallogr. Sect. F, 73, 24-28 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3)	Pseudomonas sp.

Crystallization (Commentary)

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.

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
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

Organism	UniProt	Comment	Textmining
Pseudomonas sp.	-	-	-
Pseudomonas sp. AAC	-	-	-

Purification (Commentary)

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 and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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

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

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

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.