Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.5.3.14 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.5.3.14 |
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine |
i.e. MDL72527 |
Zea mays |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.5.3.14 |
Zea mays |
O64411 |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.5.3.14 |
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]
EC Number |
Ki Value [mM] |
Ki Value maximum [mM] |
Inhibitor |
Comment |
Organism |
Structure |
---|
1.5.3.14 |
0.00055 |
- |
N,N'-bis(2,3-butadienyl)-1,4-butane-diamine |
pH 6.5, 25°C |
Zea mays |
|