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1.1.1.373: sulfolactaldehyde 3-reductase

This is an abbreviated version!
For detailed information about sulfolactaldehyde 3-reductase, go to the full flat file.

Reaction

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2,3-dihydroxypropane-1-sulfonate
+
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NAD+
=
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2-hydroxy-3-oxopropane-1-sulfonate
+
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NADH
+
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H+

Synonyms

3-sulfolactaldehyde reductase, 3-sulpholactaldehyde reductase, NADH-dependent SLA reductase, SLA reductase, sulfolactaldehyde reductase, yihU

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                EC 1.1.1.3731.1.1.373 sulfolactaldehyde 3-reductase

General Information

General Information on EC 1.1.1.373 - sulfolactaldehyde 3-reductase

for references in articles please use BRENDA:EC1.1.1.373

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
based on conserved sequence motifs, enzyme SLA reductase is assigned to the beta-hydroxyacid dehydrogenase (beta-HAD) family, comparisons of typical sequence motifs. SLA reductases form a separate subgroup with conserved sulfonate substrate-binding sequence at residues 122-124 (YihU numbering). SLA reductases share beta-HAD sequence motifs but possess a unique sulfonate substrate-binding sequence (extended motif-2 [D/EVPVGRTXX-XAXXG])
physiological function
2,3-dihydroxypropanesulfonate (DHPS) is a major sulfur species in the biosphere. One important route for the production of DHPS is sulfoglycolytic catabolism of sulfoquinovose (SQ) through the Embden-Meyerhof-Parnas (sulfo-EMP) pathway. SQ is a sulfonated carbohydrate present in plant and cyanobacterial sulfolipids (sulfoquinovosyl diacylglyceride and its metabolites) and is biosynthesized globally at a rate of around 10 billion tons per annum. The final step in the bacterial sulfo-EMP pathway involves reduction of sulfolactaldehyde (SLA) to DHPS, catalyzed by the NADH-dependent SLA reductase
additional information
a conserved sulfonate pocket in SLA reductase recognizes the sulfonate oxygens through hydrogen bonding to Asn174, Ser178, and the backbone amide of Arg123, along with an ordered water molecule. This triad of residues distinguishes these enzymes from classical beta-HADs that act on carboxylate substrates. Determination of the structural basis for cofactor binding and sulfonate recognition, dynamic structural changes occur during catalysis