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
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetyl CoA biosynthesis
-
-
beta-Alanine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
3-oxopropanoate:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-94-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain BL23
-
-
Manually annotated by BRENDA team
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
-
-
-
-
-
malonic semialdehyde + NAD+
acetyl-CoA + NADH + CO2
show the reaction diagram
-
-
-
-
?
NAD(P)+ + 3-oxopropanoate + H2O
malonate + NAD(P)H
show the reaction diagram
-
-
-
ir
additional information
?
-
-
no activity with formaldehyde, acetaldehyde, propionaldehyde, isovaleraldehyde, benzaldehyde, anisaldehyde, glyceraldehyde, glyceraldehyde-3-phosphate, glyoxylate, succinic semialdehyde
-
-
-
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
-
-
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
less than 10% activity compared with NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
increases activity 42% at 1 mM
Mg2+
-
increases activity 64% at 1 mM
Mn2+
-
increases activity 27% at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glyoxylate
-
competitive inhibitor
malonate
-
competitive inhibitor
p-chloromercuribenzoate
-
-
succinate semialdehyde
-
non-competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
Malonate semialdehyde
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
glyoxylate
-
-
0.57
malonate
-
-
0.56
succinate semialdehyde
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
-
malonate semialdehyde + NAD+
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
with NAD+ and bovine serum albumin at pH 8.7
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM mercaptoethanol is essential for stability
-
unstable in dilute solution
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 1 month
-
0°C, bovine serum albumin, NAD+, 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutated iolA gene cloned into pRV300 giving pRViolASpeI. Expressed in Lactobacillus casei
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
disruption of iolA gene provides a myo-inositol-negative strain
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
iolA is indispensable for myo-inositol fermentation