BRENDA - Enzyme Database
show all sequences of 1.2.1.18

X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC

Wilding, M.; Scott, C.; Peat, T.S.; Newman, J.; Acta Crystallogr. Sect. F 73, 24-28 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3)
Pseudomonas sp.
Crystallization (Commentary)
Crystallization (Commentary)
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 8C, 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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
Commentary
Textmining
Pseudomonas sp.
A0A081YAY7
-
-
Pseudomonas sp. AAC
A0A081YAY7
-
-
Purification (Commentary)
Purification (Commentary)
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3-oxopropanoate + CoA + NAD+
-
741539
Pseudomonas sp.
acetyl-CoA + CO2 + NADH
-
-
-
?
3-oxopropanoate + CoA + NAD+
-
741539
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
741539
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
741539
Pseudomonas sp. AAC
?
-
-
-
-
Subunits
Subunits
Commentary
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
Commentary
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
Commentary
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.
Cloned(Commentary) (protein specific)
Commentary
Organism
gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3)
Pseudomonas sp.
Cofactor (protein specific)
Cofactor
Commentary
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.
Crystallization (Commentary) (protein specific)
Crystallization
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 8C, 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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3-oxopropanoate + CoA + NAD+
-
741539
Pseudomonas sp.
acetyl-CoA + CO2 + NADH
-
-
-
?
3-oxopropanoate + CoA + NAD+
-
741539
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
741539
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
741539
Pseudomonas sp. AAC
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
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.
Other publictions for EC 1.2.1.18
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741539
Wilding
X-ray crystal structure of a ...
Pseudomonas sp., Pseudomonas sp. AAC
Acta Crystallogr. Sect. F
73
24-28
2017
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690142
Alnouti
Tissue distribution, ontogeny, ...
Mus musculus
Toxicol. Sci.
101
51-64
2008
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689379
Marchitti
Neurotoxicity and metabolism o ...
Homo sapiens
Pharmacol. Rev.
59
125-150
2007
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288061
Strauss
Enzymes of a novel autotrophic ...
Chloroflexus aurantiacus
Eur. J. Biochem.
215
633-643
1993
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288055
Goodwin
Purification and characterizat ...
Rattus norvegicus
J. Biol. Chem.
264
14965-14971
1989
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288056
Waters
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A complete pathway for beta-al ...
Pseudomonas aeruginosa
FEMS Microbiol. Lett.
34
279-282
1986
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288057
Maentsaelae
-
Formation of malonate-semialde ...
Pseudomonas fluorescens
Acta Chem. Scand.
1
395-396
1972
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288058
Jakoby
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Aldehyde dehydrogenase ...
Pseudomonas sp.
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
203-221
1963
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288059
Hayaishi
Enzymatic studies on the metab ...
Pseudomonas fluorescens
J. Biol. Chem.
236
781-790
1961
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288060
Yamada
Aldehyde oxidation ...
Pseudomonas fluorescens
J. Biol. Chem.
235
589-594
1960
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