EC Number   |
General Information |
Reference |
|---|
  1.1.1.313 | evolution |
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 |
762708 |
| 1.1.1.313 | 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 |
762706 |
| 1.1.1.313 | evolution |
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family |
-, 762832 |
| 1.1.1.313 | 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) |
-, 762832 |
| 1.1.1.313 | metabolism |
IsfD-dependent metabolic pathway and genome neighborhood of IsfD, overview |
762706 |
| 1.1.1.313 | 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 |
762708 |
| 1.1.1.313 | more |
structure-function analysis of IsfD, overview |
762708 |
| 1.1.1.313 | more |
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 |
762706 |
| 1.1.1.313 | 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 |
-, 762832 |
| 1.1.1.313 | 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 |
762706 |
