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Information on EC 1.2.1.18 - malonate-semialdehyde dehydrogenase (acetylating)
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EC Tree
1.2.1.18 malonate-semialdehyde dehydrogenase (acetylating)Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aldh6a1, methylmalonate-semialdehyde dehydrogenase, kes23460, nad-dependent malonate-semialdehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aldh6a1
dehydrogenase, malonate semialdehyde
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FG99_15390
KES23460
malonate semialdehyde oxidative decarboxylase
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malonate-semialdehyde dehydrogenase
malonate-semialdehyde dehydrogenase (NADP+) (acylating)
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malonate-semialdehyde: nicotinamide adenine dinucleotide oxidoreductase
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malonic semialdehyde oxidative decarboxylase
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methylmalonate-semialdehyde dehydrogenase
NAD-dependent malonate-semialdehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H + 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 SOURCE
PATHWAYS
BRENDA
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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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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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?
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NATURAL SUBSTRATE
NATURAL 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
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
-
?
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
?
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
ABAT and ALDH6A1, regulated by transcription factor HNF4A, suppress tumorigenic capability in clear cell renal cell carcinoma.
Carcinoma, Hepatocellular
Identification of ALDH6A1 as a Potential Molecular Signature in Hepatocellular Carcinoma via Quantitative Profiling of the Mitochondrial Proteome.
Carcinoma, Renal Cell
ABAT and ALDH6A1, regulated by transcription factor HNF4A, suppress tumorigenic capability in clear cell renal cell carcinoma.
Dehydration
Importance of inositols and their derivatives in cowpea under root dehydration: An omics perspective.
Diabetes Mellitus, Type 2
Downregulation of the acetyl-CoA metabolic network in adipose tissue of obese diabetic individuals and recovery after weight loss.
Metabolic Diseases
Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease.
Neoplasm Metastasis
Co-expression network analysis identified six hub genes in association with metastasis risk and prognosis in hepatocellular carcinoma.
Neoplasms
ABAT and ALDH6A1, regulated by transcription factor HNF4A, suppress tumorigenic capability in clear cell renal cell carcinoma.
Neoplasms
HSP27, ALDH6A1 and Prohibitin Act as a Trio-biomarker to Predict Survival in Late Metastatic Prostate Cancer.
Neoplasms
Identification of ALDH6A1 as a Potential Molecular Signature in Hepatocellular Carcinoma via Quantitative Profiling of the Mitochondrial Proteome.
Prostatic Neoplasms
HSP27, ALDH6A1 and Prohibitin Act as a Trio-biomarker to Predict Survival in Late Metastatic Prostate Cancer.
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (1427 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goodwin, G.W.; Rougraff, P.M.; Davis, E.J.; Harris, R.A.
Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase
J. Biol. Chem.
264
14965-14971
1989
Rattus norvegicus
brenda
Waters, P.; Venables, W.A.
A complete pathway for beta-alanine and beta-amino-iso-butyrate catabolism in Pseudomonas aeruginosa
FEMS Microbiol. Lett.
34
279-282
1986
Pseudomonas aeruginosa
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brenda
Maentsaelae, P.; Pirttikoski, M.; Numikko, V.
Formation of malonate-semialdehyde: nicotinamide adenine dinucleotide (NAD) oxidoreductase in Pseudomonas fluorescens P-2
Acta Chem. Scand.
1
395-396
1972
Pseudomonas fluorescens
-
brenda
Jakoby, W.B.
Aldehyde dehydrogenase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
203-221
1963
Pseudomonas sp.
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brenda
Hayaishi, O.; Nishizuka, Y.; Tatibana, M.; Takeshita, M.; Kuno, S.
Enzymatic studies on the metabolism of beta-alanine
J. Biol. Chem.
236
781-790
1961
Pseudomonas fluorescens
brenda
Yamada, E.W.; Jakoby, W.B.
Aldehyde oxidation
J. Biol. Chem.
235
589-594
1960
Pseudomonas fluorescens
brenda
Strauss, G.; Fuchs, G.
Enzymes of a novel autotrophic carbon dioxide fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle
Eur. J. Biochem.
215
633-643
1993
Chloroflexus aurantiacus
brenda
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
Pharmacol. Rev.
59
125-150
2007
Homo sapiens (Q02252)
brenda
Alnouti, Y.; Klaassen, C.D.
Tissue distribution, ontogeny, and regulation of aldehyde dehydrogenase (Aldh) enzymes mRNA by prototypical microsomal enzyme inducers in mice
Toxicol. Sci.
101
51-64
2008
Mus musculus (Q9EQ20)
brenda
Wilding, M.; Scott, C.; Peat, T.S.; Newman, J.
X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC
Acta Crystallogr. Sect. F
73
24-28
2017
Pseudomonas sp., Pseudomonas sp. AAC
brenda
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