3pgb

Publication Abstract from PubMed

Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in alpha-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 A. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.

Structure and Activity of Aspergillus nidulans Copper Amine Oxidase.,McGrath AP, Mithieux SM, Collyer CA, Bakhuis JG, van den Berg M, Sein A, Heinz A, Schmelzer C, Weiss AS, Guss JM Biochemistry. 2011 Jun 28;50(25):5718-30. Epub 2011 Jun 3. PMID:21604787^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.