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Literature summary for 1.5.3.14 extracted from

  • Binda, C.; Coda, A.; Angelini, R.; Federico, R.; Ascenzi, P.; Mattevi, A.
    A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase (1999), Structure, 7, 265-276.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallised by the hanging drop vapour-diffusion method, with the protein solution consisting of 5 mg enzyme/ml in 300 mM NaCl and 50 mM sodium phosphate buffer, pH 6.0. Crystal structure of polyamine oxidase is determined to a resolution of 1.9 A. The enzyme contains two domains, which define a remarkable 30 A long U-shaped catalytic tunnel at their interface. The structure of PAO in complex with the inhibitor MDL72527 reveals the residues forming the catalytic machinery and unusual enzyme-inhibitor CH...OH bonds. A ring of glutamate and aspartate residues surrounding one of the two tunnel openings contributes to the steering of the substrate towards the inside of the tunnel Zea mays

Inhibitors

Inhibitors Comment Organism Structure
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine i.e. MDL72527 Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays O64411
-
-

Cofactor

Cofactor Comment Organism Structure
FAD the FAD prosthetic group is non-covalently bound to the protein and is deeply embedded within the structure. All FAD atoms are solvent-inaccessible, with the exception of the flavin C5a, N5 and C4a atoms that line the active centre Zea mays

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00055
-
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine pH 6.5, 25°C Zea mays