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1.4.1.9: leucine dehydrogenase

This is an abbreviated version!
For detailed information about leucine dehydrogenase, go to the full flat file.

Word Map on EC 1.4.1.9

Reaction

L-leucine
+
H2O
 +
NAD+
=
4-methyl-2-oxopentanoate
 +
NH3
 +
NADH
 +
H+

Synonyms

BCD, dehydrogenase, leucine, L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, LeuDH

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.9 leucine dehydrogenase

Crystallization

Crystallization on EC 1.4.1.9 - leucine dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and semirational engineering to increase the catalytic efficiency
-
modeling of structure. Active site residues Lys81, Asp116, and Lys69 are catalytically important. Lys81 linkes the -OH group of the substrate 2-oxobutanoate by a 2.3-A long H-bond, and Asp116 is involved in proton transfer during catalysis
-
cryo-electron microscopy structures of apo and NAD+-bound LDH at 3.0 and 3.2 A resolution, respectively. A partial conformational change is triggered by the interaction between Ser147 and the nicotinamide moiety of NAD+. NAD+ binding also enhances the strength of oligomerization interfaces formed by the core domains
structure of apo-protein and in complex with NAD+, to 3.0 and 3.2 A resolution, respectively. NAD+ binds to domain II (residues 137-331), and the NAD+-bound form has a disordered region (residues 142-144) in the loop between domains I and II
A0A0K2HC96
crystallized by addition of ammonium sulfate
-
hanging drop method of vapour diffusion, using ammonium sulfate as the precipitant
-
homology modeling of structure. Enzyme exhibits several cold-adapted features
crystals of the binary complex with 4-methyl-2-oxopentanoate, hanging-drop vapour-diffusion method using PEG 4000 as precipitant
-