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4.1.1.22: histidine decarboxylase

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

Word Map on EC 4.1.1.22

Reaction

L-histidine
=
histamine
+
CO2

Synonyms

DCHS, Decarboxylase, histidine, HDC, HdcA, HisDCase, histamine-forming enzyme, L-Histidine decarboxylase, pyruvoyl-dependent decarboxylase, pyruvoyl-dependent histidine decarboxylase, TOM92

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.22 histidine decarboxylase

Crystallization

Crystallization on EC 4.1.1.22 - histidine decarboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
core domain, to 1.8 A resolution. Three dimers per asymmetric unit. Molecular replacement carried out using the AroDC structure as a model
in complex with the inhibitor histidine methyl ester, to 1.8 A resolution. Cofactor pyridoxal 5'-phosphate is located in the large domain. The pyridine ring of pyridoxal 5'-phosphate is sandwiched between the methyl group of Ala275 and the imidazole ring of His194. Residue Ser354 is a key residue for substrate specificity
crystal structure at 3.0 A resolution
-
crystal structure of active HDC at pH 4.8 at 2.5 A resolution, crystal structure of less active HDC at pH 8.0 at 2.7 A resolution, crystals are grown at room temperatur by hanging-drop vapor diffusion, drops contain 0.004 ml HDC at 12.5 mg/ml, 0.001 ml n-dodecyl-beta-D-maltoside and 0.005 ml precipitant solution from the well containing 25% polyethylene glycol 400, 8% polyethylene glycol 400, 100 mM Tris pH 8.0, and 100 mM sodium acetate, enzyme activity is regulated by pH-induced structural changes
modeling of complex with inhibitor epigallocatechin-3-gallate. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses
-