1.1.1.337: L-2-hydroxycarboxylate dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about L-2-hydroxycarboxylate dehydrogenase (NAD+), go to the full flat file.

Word Map on EC 1.1.1.337

Reaction

a (2S)-2-hydroxycarboxylate
+
NAD+
=
a 2-oxocarboxylate
+
NADH
+
H+

Synonyms

(R)-sulfolactate dehydrogenase, ComC, L-2-hydroxyacid dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), L-2-hydroxyisocaproate dehydrogenase, L-HicDH, L-hydroxyisocaproate dehydrogenase, L-sulfolactate dehydrogenase, MDH I, MJ1425, sulfolactate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.337 L-2-hydroxycarboxylate dehydrogenase (NAD+)

Crystallization

Crystallization on EC 1.1.1.337 - L-2-hydroxycarboxylate dehydrogenase (NAD+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NADH, to 2.5 A resolution. The asymmetric unit contains a tetramer of tight dimers. Structure does not contain a cofactor-binding domain with Rossmann-fold topology. The NADH is bound in an extended conformation in each active site, in a manner that explains the pro-S specificity. Cofactor binding involves residues belonging to both subunits within the tight dimers. The results indicate the existence of a substrate discrimination mechanism, which involves electrostatic interactions
recombinant enzyme is crystallized with ammonium sulfate as precipitant in the presence of NAD+. The crystals belong to the trigonal space group P3(2)21, with a = 135.9 A and c = 205.9 A, and diffract X-rays to 2.2 A resolution