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Information on EC 1.2.1.18 - malonate-semialdehyde dehydrogenase (acetylating)
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.2.1.18
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RECOMMENDED NAME
GeneOntology No.
malonate-semialdehyde dehydrogenase (acetylating)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating)
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CAS REGISTRY NUMBER
COMMENTARY
9028-97-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methyl-3-oxopropanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
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both stereoisomers
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?
3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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enzyme is involved in catabolism of beta-alanine
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?
3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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inducible enzyme, beta-alanine seems to be the real inducer
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?
malonyl-CoA + NADPH
malonate-semialdehyde + CoA + NADP+
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?
malonyl-CoA + NADPH
malonate-semialdehyde + CoA + NADP+
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enzyme is involved in the autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
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?
additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + NADPH
malonate-semialdehyde + CoA + NADP+
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enzyme is involved in the autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
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?
3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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enzyme is involved in catabolism of beta-alanine
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?
3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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inducible enzyme, beta-alanine seems to be the real inducer
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?
additional information
?
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A0A081YAY7
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
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-
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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
-
-
-
additional information
?
-
A0A081YAY7
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
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.7
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pH 6.0: about 35% of maximal activity, pH 7.7: about 65% of maximal activity, activity with NADP+
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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
tetramer
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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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against phosphate buffer, pH 7.0, for 4 h at 4°C results in 80% loss of activity
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freezing and thawing causes total loss of activity even in the presence of 0.01 M 2-mercaptoethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, pH 7.0, in presence of 2-mercaptoethanol, stored with least loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration to over 95% purity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.18)
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