1KSI

CRYSTAL STRUCTURE OF A EUKARYOTIC (PEA SEEDLING) COPPER-CONTAINING AMINE OXIDASE AT 2.2A RESOLUTION

Summary for 1KSI

• Entry DOI: 10.2210/pdb1ksi/pdb
• Descriptor: COPPER AMINE OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: oxidase, pea seedling, oxidoreductase
• Biological source: Pisum sativum (pea)
• Total number of polymer chains: 2
• Total formula weight: 147627.56

Authors

Wilce, M.C.J.,Kumar, V.,Freeman, H.C.,Guss, J.M. (deposition date: 1996-07-20, release date: 1997-12-24, Last modification date: 2024-12-25)

Primary citation

Kumar, V.,Dooley, D.M.,Freeman, H.C.,Guss, J.M.,Harvey, I.,McGuirl, M.A.,Wilce, M.C.,Zubak, V.M.
Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution.
Structure, 4:943-955, 1996

PubMed Abstract: Copper-containing amine oxidases catalyze the oxidative deamination of primary amines to aldehydes, in a reaction that requires free radicals. These enzymes are important in many biological processes, including cell differentiation and growth, would healing, detoxification and signalling. The catalytic reaction requires a redox cofactor, topa quinone (TPQ), which is derived by post-translational modification of an invariant tyrosine residue. Both the biogenesis of the TPQ cofactor and the reaction catalyzed by the enzyme require the presence of a copper atom at the active site. The crystal structure of a prokaryotic copper amine oxidase from E. coli (ECAO) has recently been reported.

PubMed: 8805580
DOI: 10.1016/S0969-2126(96)00101-3

Experimental method

X-RAY DIFFRACTION (2.2 Å)