Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.15 gene KES23460, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas sp.
1.2.1.18 gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas sp.
1.2.1.27 gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.15 purified recombinant enzyme, method screening, crystallization of 20 mg/ml protein with crystalliztaion solution consisting of 1.38 M ammonium sulfate, 3.35% 2,2,2-trifluoroethanol, 2% benzamidine, the resulting crystals are used for microseding with 5 mg/ml protein, 1 mM acetyl-CoA, and a solution containing 23.7% w/v PEG 3350, 0.208 M trisodium citrate, 0.1 M Bis-Tris propane, pH 7.55, at 8°C, method optimization, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement using structure with PDB ID 4zz7 as the search model Pseudomonas sp.
1.2.1.18 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.
1.2.1.27 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.18 3-oxopropanoate + CoA + NAD+ Pseudomonas sp.
-
acetyl-CoA + CO2 + NADH
-
?
1.2.1.18 3-oxopropanoate + CoA + NAD+ Pseudomonas sp. AAC
-
acetyl-CoA + CO2 + NADH
-
?
1.2.1.18 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 ?
-
?
1.2.1.18 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 ?
-
?
1.2.1.27 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 ?
-
?
1.2.1.27 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

EC Number Organism UniProt Comment Textmining
1.2.1.15 Pseudomonas sp.
-
-
-
1.2.1.15 Pseudomonas sp. AAC
-
-
-
1.2.1.18 Pseudomonas sp.
-
-
-
1.2.1.18 Pseudomonas sp. AAC
-
-
-
1.2.1.27 Pseudomonas sp.
-
-
-
1.2.1.27 Pseudomonas sp. AAC
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.15 recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration to over 95% purity Pseudomonas sp.
1.2.1.18 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration to over 95% purity Pseudomonas sp.
1.2.1.27 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.18 3-oxopropanoate + CoA + NAD+
-
Pseudomonas sp. acetyl-CoA + CO2 + NADH
-
?
1.2.1.18 3-oxopropanoate + CoA + NAD+
-
Pseudomonas sp. AAC acetyl-CoA + CO2 + NADH
-
?
1.2.1.18 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. ?
-
?
1.2.1.18 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 ?
-
?
1.2.1.27 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. ?
-
?
1.2.1.27 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

EC Number Subunits Comment Organism
1.2.1.15 hexamer
-
Pseudomonas sp.
1.2.1.18 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.
1.2.1.27 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

EC Number Synonyms Comment Organism
1.2.1.15 KES23460
-
Pseudomonas sp.
1.2.1.15 NAD-dependent malonate-semialdehyde dehydrogenase
-
Pseudomonas sp.
1.2.1.18 FG99_15390
-
Pseudomonas sp.
1.2.1.18 KES23460
-
Pseudomonas sp.
1.2.1.18 malonate-semialdehyde dehydrogenase
-
Pseudomonas sp.
1.2.1.18 methylmalonate-semialdehyde dehydrogenase UniProt Pseudomonas sp.
1.2.1.18 NAD-dependent malonate-semialdehyde dehydrogenase
-
Pseudomonas sp.
1.2.1.27 FG99_15390
-
Pseudomonas sp.
1.2.1.27 KES23460
-
Pseudomonas sp.
1.2.1.27 malonate-semialdehyde dehydrogenase
-
Pseudomonas sp.
1.2.1.27 methylmalonate-semialdehyde dehydrogenase UniProt Pseudomonas sp.
1.2.1.27 NAD-dependent malonate-semialdehyde dehydrogenase
-
Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.15 NAD+
-
Pseudomonas sp.
1.2.1.18 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.
1.2.1.27 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.

General Information

EC Number General Information Comment Organism
1.2.1.15 physiological function the enzyme is involved in the beta-alanine catabolism to produce acetyl-CoA Pseudomonas sp.