1.1.1.387: L-serine 3-dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about L-serine 3-dehydrogenase (NAD+), go to the full flat file.

Reaction

2-aminomalonate semialdehyde
=
2-aminoacetaldehyde
+
CO2

Synonyms

NAD+-dependent L-serine dehydrogenase, PA0743

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.387 L-serine 3-dehydrogenase (NAD+)

Crystallization

Crystallization on EC 1.1.1.387 - L-serine 3-dehydrogenase (NAD+)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
two crystal structures of the enzyme are solved at 2.2-2.3 A resolution and reveal an N-terminal Rossmann fold domain connected by a long alpha-helix to the C-terminal all-alpha-domain. The apostructure shows the presence of additional density modeled as HEPES bound in the interdomain cleft close to the predicted catalytic Lys171, revealing the molecular details of the enzyme substrate-binding site. The structure of the enzyme-NAD complex demonstrates that the opposite side of the enzyme active site accommodates the cofactor, which is also bound near Lys171. Crystals of the enzyme are grown at 21C by the hanging drop vapor diffusion method with 0.002 ml of protein sample mixed with an equal volume of the reservoir buffer. The crystals of the wild-type enzyme grew after 1 week in the presence of 4 M ammonium acetate and 0.1 M sodium acetate (pH 5.4). The crystals of the complex of the enzyme with NAD+ are obtained by soaking the crystals in 10 mM NAD+. For diffraction studies, the crystals are stabilized with the crystallization buffer supplemented with 12% ethylene glycol as a cryoprotectant and flash frozen in liquid nitrogen