6smz

Structural highlights

Function

SQUU_ECOLI Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS) (PubMed:24463506, Ref.6). Metabolite profiling studies showed that the enzyme also catalyzes in vitro the NADH-dependent reduction of succinic semialdehyde (SSA) to 4-hydroxybutyrate (GHB), and that it could be involved in the metabolism of SSA, and other potentially toxic intermediates that may accumulate under stress conditions (PubMed:19372223). However, the enzyme exhibits a 42,000-fold greater catalytic efficiency for the reduction of SLA over SSA (Ref.6). Shows no detectable activity on the analogous glycolytic intermediate glyceraldehyde-3-phosphate (Ref.6).^{[1] [2] [3]}

References

1. ↑ Saito N, Robert M, Kochi H, Matsuo G, Kakazu Y, Soga T, Tomita M. Metabolite profiling reveals YihU as a novel hydroxybutyrate dehydrogenase for alternative succinic semialdehyde metabolism in Escherichia coli. J Biol Chem. 2009 Jun 12;284(24):16442-16451. PMID:19372223 doi:10.1074/jbc.M109.002089
2. ↑ Denger K, Weiss M, Felux AK, Schneider A, Mayer C, Spiteller D, Huhn T, Cook AM, Schleheck D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature. 2014 Mar 6;507(7490):114-7. doi: 10.1038/nature12947. Epub 2014 Jan 26. PMID:24463506 doi:http://dx.doi.org/10.1038/nature12947
3. ↑ Denger K, Weiss M, Felux AK, Schneider A, Mayer C, Spiteller D, Huhn T, Cook AM, Schleheck D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature. 2014 Mar 6;507(7490):114-7. doi: 10.1038/nature12947. Epub 2014 Jan 26. PMID:24463506 doi:http://dx.doi.org/10.1038/nature12947