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Literature summary for 1.1.1.313 extracted from

  • Rohwerder, T.
    New structural insights into bacterial sulfoacetaldehyde and taurine metabolism (2020), Biochem. J., 477, 1367-1371 .
    View publication on PubMed
Search for more literature for 1.1.1.313

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-sulfoacetaldehyde + NADPH + H+ Klebsiella oxytoca
-
 isethionate + NADP+
-
 r

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca D3U1D9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-sulfoacetaldehyde + NADPH + H+
-
 Klebsiella oxytoca isethionate + NADP+
-
 r

Subunits

Subunits Comment Organism
homotetramer in the tetrameric structure of IsfD, the respective diagonal subunits cross-interact strongly via their C-terminal tails. The latter region with beta-sheets 8 and 9 protrudes away from the main subunit body and reaches the active site of the opposite subunit. Thus, stabilization of the substrate-binding loop in the closed conformation is accomplished. In particular, C-terminal residue F248 is located close to side chains of active site amino acids I142 and Y148 of the diagonal subunit. This important interaction results in a proper positioning of Y148 for hydrogen bonding with the sulfonate group of isethionate. Enzyme structure comparisons, detailed overview Klebsiella oxytoca

Synonyms

Synonyms Comment Organism
IsfD
-
 Klebsiella oxytoca

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Klebsiella oxytoca
NADPH binding structure analysis from crystal structure (PDB ID 6IXJ) Klebsiella oxytoca

General Information

General Information Comment Organism
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 Klebsiella oxytoca
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 Klebsiella oxytoca
additional information structure-function analysis of IsfD, overview Klebsiella oxytoca
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 Klebsiella oxytoca