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EC Tree
IUBMB Comments This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
The enzyme appears in viruses and cellular organisms
Synonyms
sulfoacetaldehyde dehydrogenase, nad-coupled sulfoacetaldehyde dehydrogenase,
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NAD-coupled sulfoacetaldehyde dehydrogenase
additional information
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the enzyme belongs to the NAD-dependent aldehyde dehydrogenase superfamily
NAD-coupled sulfoacetaldehyde dehydrogenase
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NAD-coupled sulfoacetaldehyde dehydrogenase
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2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+
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2-sulfoacetaldehyde:NAD+ oxidoreductase
This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NAD(P)H + H+
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the enzyme is specific for sulfoacetaldehyde, NAD+ is the highly preferred cofactor to NADP+
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
additional information
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the organism assimilates taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter, taurine:pyruvate aminotransferase, a sulfoacetaldehyde dehydrogenase, and exporter(s) of sulfoacetate, overview
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
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NAD+ is the highly preferred cofactor
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
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NAD+ is the highly preferred cofactor
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
additional information
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the organism assimilates taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter, taurine:pyruvate aminotransferase, a sulfoacetaldehyde dehydrogenase, and exporter(s) of sulfoacetate, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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NAD+
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NAD+
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highly preferred cofactor
NAD+
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highly preferred cofactor
NADP+
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low activity
NADP+
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low activity and inhibition at higher concentration
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Mg2+
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NADP+
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low activity an inhibition at higher concentration
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0.026
2-sulfoacetaldehyde
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pH 9.0, 22°C
0.49
Sulfoacetaldehyde
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pH 9.0, 22°C
0.092
NAD+
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pH 9.0, 22°C
4.5
NADP+
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pH 9.0, 22°C
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9
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7.2 - 10.5
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50% of maximal activity at pH 7.2, 70% at pH 8.0, and 80% at pH 9.5-10.5
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22
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assay at room temperature
22
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assay at room temperature
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formerly Oceanospirillum sp., CCUG 52065, a marine gammaproteobacterium, strain MED92, gene safD encoding an inducible enzyme
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brenda
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growth with taurine (2-aminoethanesulfonate) as the sole source of combined nitrogen under aerobic conditions
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growth with taurine (2-aminoethanesulfonate) as the sole source of combined nitrogen under aerobic conditions
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196500
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sequence calculation
49100
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
50000
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
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tetramer
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
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SafD is stable in Tris-HCl buffer, pH 9.0
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native enzyme 610fold to homogeneity by anion exchange and hydrophobic interaction chromatography
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gene safD, DNA and amino acid sequence determination and analysis, genetic organization
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analysis
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the enzyme is useful for determination of sulfoacetaldehyde concentrations
analysis
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the enzyme is useful for determination of sulfoacetaldehyde concentrations
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Weinitschke, S.; von Rekowski, K.S.; Denger, K.; Cook, A.M.
Sulfoacetaldehyde is excreted quantitatively by Acinetobacter calcoaceticus SW1 during growth with taurine as sole source of nitrogen
Microbiology
151
1285-1290
2005
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
brenda
Denger, K.; Weinitschke, S.; Hollemeyer, K.; Cook, A.M.
Sulfoacetate generated by Rhodopseudomonas palustris from taurine
Arch. Microbiol.
182
254-258
2004
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
brenda
Krejcik, Z.; Denger, K.; Weinitschke, S.; Hollemeyer, K.; Paces, V.; Cook, A.M.; Smits, T.H.
Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase
Arch. Microbiol.
190
159-168
2008
Neptuniibacter caesariensis
brenda
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1.2.1.73 sulfoacetaldehyde dehydrogenase
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