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1.4.1.1: alanine dehydrogenase

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

Word Map on EC 1.4.1.1

Reaction

L-alanine
+
H2O
 +
NAD+
=
pyruvate
 +
NH3
 +
NADH
 +
H+

Synonyms

(S)alanine dehydrogenase, (S)alanine:NAD oxidoreductase, 40 kDa antigen, ADH, AF1665, ALADH, alanine dehydrogenase, alanine oxidative deaminase, alanine oxidoreductase, ALD, AldA, alpha-alanine dehydrogenase, ApalaDH, AsAlaDH, CQA66_00465, dehydrogenase, alanine, glyoxylate reductive aminase, GxrA, HAADH1, HAADH2, L-Ala dehydrogenase, L-AlaDH, L-AlaDH-Bs, L-alanine dehydrogenase, MtbALD, NAD(H)-dependent L-alanine dehydrogenase, NAD+ dependent amino acid dehydrogenase, NAD+-dependent alanine dehydrogenase, NAD-dependent alanine dehydrogenase, NAD-linked alanine dehydrogenase, NADH-dependent alanine dehydrogenase, OF4Ald, PlaAlaDH, PvRA, pyruvate reductive aminase, Rv2780, ScALD, SCO1773, SheAlaDH, TB43

ECTree

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

Crystallization

Crystallization on EC 1.4.1.1 - alanine dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.8 A resoution, triclinic space group P1
Alkalihalophilus pseudofirmus
crystal structure of the NAD-bound enzyme at 2.3 A in a C2 crystal form with the 70000 Da dimer in the asymmetric unit
hanging-drop vapour diffusion method. Crystallized in several forms. One polymorph growing in space group P2(1)2(1)2(1) has non-crystallographic symmetry that becomes crystallographic, changing the space group to P2(1)2(1)2(1) upon binding iridium or samarium
-
structure of the NAD+-bound AF1665 AlaDH at 2.3 A in a C2 crystal form with the 70000 Da dimer as the asymmetric unit
hanging drop vapour diffusion method, crystals of apo-AlaDH are grown using 0.4 M ammonium hydrogenphosphate as reservoir solution at 20°C
-
identificaion of putative inhibitors by molecular docking
investigation of functional domain motions by using the Gaussian network model and the anisotropy network model. The domain motions have a common hinge axis centered in residues Met133 and Met301. Both the NAD-binding domain and the substrate-binding domain move in a highly coupled way. The first three slowest modes exhibit the open-closed, rotation and twist motions
using the hanging-drop method crystal structures of the apo enzyme as also a ternary complex with NAD and pyruvate is reported. Each chain of the enzyme can be divided into catalytic and NAD-binding domains, respectively. The individual subunits associate into a hexamer with the catalytic domains on the outside as observed in the apo and holo enzyme crystals. The structures have captured open and closed conformations of the enzyme and clarify that a domain rearrangement step must take place during the reaction as opposed to alterations in intersubunit interactions
hanging-drop method
-
purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, mixed with 0.1 M HEPES, pH 8.0, 12% w/v PEG 8000, and 8% v/v ethylene glycol, 4°C, method optimization, X-ray diffraction structure determination and analysis at 2.35 A resolution