Open AccessA new crystal form of human diamine oxidase
Author(s) -
McGrath Aaron P.,
Hilmer Kimberly M.,
Collyer Charles A.,
Dooley David M.,
Guss J. Mitchell
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109052130
Subject(s) - diamine oxidase , oxidative deamination , diamine , amine gas treating , amine oxidase , chemistry , molecule , deamination , substrate (aquarium) , enzyme , stereochemistry , biochemistry , organic chemistry , biology , ecology
Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1–3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P 2 1 2 1 2 1 with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 Å resolution in space group C 222 1 with one molecule in the asymmetric unit is reported.