Open AccessThe copper‐containing amine oxidase from Arthrobacter globiformis : refinement at 1.55 and 2.20 Å resolution in two crystal forms
Author(s) -
Langley David B.,
Duff Anthony P.,
Freeman Hans C.,
Guss J. Mitchell
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106038814
Subject(s) - amine oxidase , chemistry , amine gas treating , copper , arthrobacter , crystal structure , hydrogen peroxide , residue (chemistry) , cofactor , amine oxidase (copper containing) , stereochemistry , polymer chemistry , crystallography , enzyme , diamine oxidase , organic chemistry
Copper‐containing amine oxidases are found in all the major kingdoms of life. They catalyse the oxidation of organic amines in the presence of molecular dioxygen to aldehydes and hydrogen peroxide. The catalytic centres contain a Cu atom and a topaquinone cofactor formed autocatalytically from a tyrosine residue in the presence of Cu and molecular oxygen. The structure of the Cu‐containing amine oxidase from Arthrobacter globiformis , which was previously refined at 1.8 Å resolution in space group C 2 with unit‐cell parameters a = 157.84, b = 63.24, c = 91.98 Å, β = 112.0° [Wilce et al. (1997), Biochemistry , 36 , 16116–16133], has been re‐refined with newly recorded data at 1.55 Å resolution. The structure has also been solved and refined at 2.2 Å resolution in a new crystal form, space group C 2, with unit‐cell parameters a = 158.04, b = 64.06, c = 69.69 Å, β = 111.7°.