1.1.1.313: sulfoacetaldehyde reductase (NADPH)
This is an abbreviated version!
For detailed information about sulfoacetaldehyde reductase (NADPH), go to the full flat file.
Reaction
Synonyms
isethionate formation, reductase D, IsfD, IsfD2, NADPH-dependent sulfoacetaldehyde reductase
ECTree
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General Information
General Information on EC 1.1.1.313 - sulfoacetaldehyde reductase (NADPH)
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evolution
metabolism
physiological function
additional information
among the dehydrogenases and reductases from taurine metabolism, only IsfD belongs to the short-chain dehydrogenase/reductase (SDR) superfamily. IsfD is closely related to YdfG from Escherichia coli (49% identical residues at 97% query cover) that has been characterized at first as serine dehydrogenase but functions also as malonic semialdehyde reductase in vivo
evolution
sulfoacetaldehyde reductase (IsfD) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily, involved in nitrogen assimilation from aminoethylsulfonate (taurine) in certain environmental and human commensal bacteria. Biochemical investigations of the substrate scope of IsfD, and bioinformatics analysis of IsfD homologs, suggest that IsfD is related to the promiscuous 3-hydroxyacid dehydrogenases with diverse metabolic functions
evolution
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
evolution
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the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE)
metabolism
IsfD-dependent metabolic pathway and genome neighborhood of IsfD, overview
metabolism
the enzyme catalyzes the reversible reduction in sulfoacetaldehyde to the corresponding alcohol isethionate. This is a key step in detoxification of the carbonyl intermediate formed in bacterial nitrogen assimilation from the alpha-aminoalkanesulfonic acid taurine. Bacterial taurine degradation is widespread, bacterial pathways for the degradation of taurine, overview
metabolism
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in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE)
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metabolism
-
in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE)
-
metabolism
-
in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE)
-
metabolism
-
in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE)
-
metabolism
-
in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE)
-
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut
physiological function
IsfD catalyzes the reversible NADPH-dependent reduction of sulfoacetaldehyde, which is generated by transamination of taurine, forming hydroxyethylsulfonate (isethionate) as a waste product
physiological function
like other aldehydes, sulfoacetaldehyde is potentially toxic and can be oxidized to sulfoacetate. In most taurine-degrading bacteria, however, it is reduced to the corresponding alcohol isethionate. In case this alcohol is excreted as the end product of taurine catabolism, the sulfur and carbon atoms are not assimilated. Although catalyzing serine and 3-hydroxypropionate oxidation as well, the role of IsfD in taurine metabolism and sulfoacetaldehyde reduction to isethionate is clearly corroborated by the operon-like association of the corresponding gene isfD together with genes encoding taurine uptake by transporter TauABC and deamination by transaminase Toa in Klebsiella oxytoca. There are physiological roles of IsfD-related SDR 3-hydroxyacid dehydrogenases
physiological function
-
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut
-
physiological function
-
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut
-
physiological function
-
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut
-
physiological function
-
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut
-
physiological function
-
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut
-
structure-function analysis of IsfD, overview
additional information
the bound isethionate is oriented with its hydroxyl group facing the tyrosine residue of the catalytic tetrad (Y154) and its sulfonate group forming hydrogen bond network with Y148, R195, Q244 and a water molecule. The side chains of I142, I186 and F191 further stabilize the conformation of the substrate through hydrophobic interactions. Active site structure and structure comparisons, overview