Information on EC 1.2.1.15 - malonate-semialdehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.15
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RECOMMENDED NAME
GeneOntology No.
malonate-semialdehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-oxopropanoate + NAD(P)+ + H2O = malonate + NAD(P)H + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetyl CoA biosynthesis
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beta-Alanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
3-oxopropanoate:NAD(P)+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-94-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-oxopropanoate + NAD+ + H2O
malonate + NADH
show the reaction diagram
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malonic semialdehyde + NAD+
acetyl-CoA + NADH + CO2
show the reaction diagram
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-
-
-
?
NAD(P)+ + 3-oxopropanoate + H2O
malonate + NAD(P)H
show the reaction diagram
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ir
additional information
?
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no activity with formaldehyde, acetaldehyde, propionaldehyde, isovaleraldehyde, benzaldehyde, anisaldehyde, glyceraldehyde, glyceraldehyde-3-phosphate, glyoxylate, succinic semialdehyde
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-oxopropanoate + NAD+ + H2O
malonate + NADH
show the reaction diagram
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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less than 10% activity compared with NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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increases activity 42% at 1 mM
Mg2+
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increases activity 64% at 1 mM
Mn2+
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increases activity 27% at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glyoxylate
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competitive inhibitor
malonate
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competitive inhibitor
p-chloromercuribenzoate
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succinate semialdehyde
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non-competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
Malonate semialdehyde
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
glyoxylate
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0.57
malonate
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0.56
succinate semialdehyde
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
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malonate semialdehyde + NAD+
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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with NAD+ and bovine serum albumin at pH 8.7
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM mercaptoethanol is essential for stability
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unstable in dilute solution
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 1 month
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0°C, bovine serum albumin, NAD+, 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration to over 95% purity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene KES23460, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
mutated iolA gene cloned into pRV300 giving pRViolASpeI. Expressed in Lactobacillus casei
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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disruption of iolA gene provides a myo-inositol-negative strain
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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iolA is indispensable for myo-inositol fermentation