Format

Send to:

Choose Destination
See comment in PubMed Commons below
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):137-42. doi: 10.1107/S1744309109052130. Epub 2010 Jan 27.

A new crystal form of human diamine oxidase.

Author information

  • 1School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia. a.mcgrath@mmb.usyd.edu.au

Abstract

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 P2(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 A resolution in space group C222(1) with one molecule in the asymmetric unit is reported.

PMID:
20124708
[PubMed - indexed for MEDLINE]
PMCID:
PMC2815678
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for International Union of Crystallography Icon for PubMed Central
    Loading ...
    Write to the Help Desk