Literature summary for 1.4.3.22 extracted from

Langley, D.B.; Trambaiolo, D.M.; Duff, A.P.; Dooley, D.M.; Freeman, H.C.; Guss, J.M.
Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine (2008), Acta Crystallogr. Sect. F, 64, 577-583.

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Cloned(Commentary)

Cloned (Comment)	Organism
AGAO is overexpressed recombinantly as a C-terminal Strep-tagII fusion protein	Arthrobacter globiformis

Crystallization (Commentary)

Crystallization (Comment)	Organism
complexes of amine oxidase with the inhibitors benzylhydrazine and tranylcypromine are refined at 1.86 and 1.65 A resolution, respectively. Both inhibitors form covalent adducts with the 2,4,5-trihydroxyphenylalanine quinone cofactor. Tyrosine residue 296, proposed to act as a gate to the AGAO active site, is in its open conformation	Arthrobacter globiformis

Inhibitors

Inhibitors	Comment	Organism	Structure
benzylhydrazine	-	Arthrobacter globiformis
tranylcypromine	-	Arthrobacter globiformis

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	-	-	-

Synonyms

Synonyms	Comment	Organism
AGAO	-	Arthrobacter globiformis
Amine oxidase	-	Arthrobacter globiformis

Cofactor

Cofactor	Comment	Organism	Structure
2,4,5-trihydroxyphenylalanine quinone	-	Arthrobacter globiformis

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Release 2023.1 (January 2023)