Abstract
Complexes of Arthrobacter globiformis amine oxidase (AGAO) with the inhibitors benzylhydrazine and tranylcypromine (an antidepressant drug) have been refined at 1.86 and 1.65 A resolution, respectively. Both inhibitors form covalent adducts with the TPQ cofactor. A tyrosine residue, proposed to act as a gate to the AGAO active site, is in its open conformation.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amine Oxidase (Copper-Containing) / antagonists & inhibitors
-
Amine Oxidase (Copper-Containing) / chemistry*
-
Arthrobacter / drug effects
-
Arthrobacter / enzymology*
-
Bacterial Proteins / antagonists & inhibitors
-
Bacterial Proteins / chemistry*
-
Catalytic Domain / drug effects
-
Crystallography, X-Ray
-
Enzyme Inhibitors / chemistry*
-
Hydrazines / chemistry*
-
Tranylcypromine / chemistry*
Substances
-
Bacterial Proteins
-
Enzyme Inhibitors
-
Hydrazines
-
Tranylcypromine
-
benzylhydrazine
-
Amine Oxidase (Copper-Containing)