Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

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

Subunits

Subunits on EC 1.1.1.373 - sulfolactaldehyde 3-reductase

for references in articles please use BRENDA:EC1.1.1.373

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 30000, calculated from amino acid sequence
tetramer
YihU forms a dimer of intimate homodimer pairs. The enzyme exuĆ­sts as a tetramer in crystal and in solution. Within the asymmetric unit, each protomer adopts a two-domain architecture containing an N-terminal nucleotide-binding domain (residues 1-164) and a C-terminal helical bundle (residues 165-294) both connected by the long interdomain helix alpha8. The N-terminal domain is composed of a classical alpha/beta Rossmann fold (composed of an extended sheet formed by beta1-6, flanked by alpha1-5 in a three-layered sandwich) appended with an additional beta-alpha-beta motif containing beta7-9 and alpha6. Four interfaces are present within the subunits of the YihU tetramer. Detailed structure analysis, overview