PMID: 19764817

 

    Legend: Gene, Sites

Title : Structure and inhibition of human diamine oxidase

Abstract :

1. Humans have three functioning genes that encode copper-containing amine oxidases
2. The product of the AOC1 gene is a so-called diamine oxidase ( hDAO ), named for its substrate preference for diamines, particularly histamine
3. hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A
4. The homodimeric structure has the archetypal amine oxidase fold
5. Two active sites , one in each subunit , are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine
6. Although hDAO shares 37.9% sequence identity with another human copper amine oxidase , semicarbazide sensitive amine oxidase or vascular adhesion protein-1 , its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities
7. The structures of two inhibitor complexes of hDAO , berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively
8. They bind noncovalently in the active-site channel
9. The inhibitor binding suggests that an aspartic acid residue , conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates

Output (sent_index, trigger, protein, sugar, site):

Output(Part-Of) (sent_index, protein, site):

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX