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EC Tree
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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dehydrogenase, malonate semialdehyde
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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
Aldh6a1
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FG99_15390
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KES23460
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malonate-semialdehyde dehydrogenase
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malonate-semialdehyde dehydrogenase
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methylmalonate-semialdehyde dehydrogenase
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UniProt
methylmalonate-semialdehyde dehydrogenase
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UniProt
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NAD-dependent malonate-semialdehyde dehydrogenase
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NAD-dependent malonate-semialdehyde dehydrogenase
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3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H + H+
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3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating)
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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
3-oxopropanoate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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malonyl-CoA + NADPH
malonate-semialdehyde + CoA + NADP+
additional information
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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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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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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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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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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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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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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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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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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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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3-oxopropanoate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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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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NAD+
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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
NADP+
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cofactor
NADPH
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cofactor
NADPH
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no activity with NADH
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NADH
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NADH
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competitive with NAD+
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2-mercaptoethanol
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0.1 M required for maximal activity
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Atherosclerosis
Common dysregulated pathways in obese adipose tissue and atherosclerosis.
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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0.0053
2-Methyl-3-oxopropanoate
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0.0045 - 0.05
3-oxopropanoate
0.0045
3-oxopropanoate
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0.03
CoA
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0.15
NAD+
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additional information
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additional information
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5.5 - 6
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activity with NADP+
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with NADP+
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with NAD+
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reaction with 2-methyl-3-oxopropanoate
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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+
7 - 9
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about 65% of maximal activity at pH 7.0 and at pH 9.0
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SwissProt
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UniProt
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PAO1
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isozyme Aldh6a1 mRNA expression is highest in liver
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58000
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4 * 58000, SDS-PAGE
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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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tetramer
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4 * 58000, SDS-PAGE
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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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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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2°C, pH 7.0, in presence of 2-mercaptoethanol, stored with least loss of activity
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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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gene FG99_15390, recombinant expression of the codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3)
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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.
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14965-14971
1989
Rattus norvegicus
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Waters, P.; Venables, W.A.
A complete pathway for beta-alanine and beta-amino-iso-butyrate catabolism in Pseudomonas aeruginosa
FEMS Microbiol. Lett.
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279-282
1986
Pseudomonas aeruginosa
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Maentsaelae, P.; Pirttikoski, M.; Numikko, V.
Formation of malonate-semialdehyde: nicotinamide adenine dinucleotide (NAD) oxidoreductase in Pseudomonas fluorescens P-2
Acta Chem. Scand.
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395-396
1972
Pseudomonas fluorescens
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Jakoby, W.B.
Aldehyde dehydrogenase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
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203-221
1963
Pseudomonas sp.
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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
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Yamada, E.W.; Jakoby, W.B.
Aldehyde oxidation
J. Biol. Chem.
235
589-594
1960
Pseudomonas fluorescens
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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
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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)
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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)
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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
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24-28
2017
Pseudomonas sp., Pseudomonas sp. AAC
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