1.5.3.14: polyamine oxidase (propane-1,3-diamine-forming)

This is an abbreviated version!
For detailed information about polyamine oxidase (propane-1,3-diamine-forming), go to the full flat file.

Reaction

Synonyms

EC 1.5.3.11, flavin-containing polyamine oxidase, maize PAO, maize polyamine oxidase, MPAO, OsPAO7, PAO, ZmPAO

ECTree

     1 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.3 With oxygen as acceptor

                1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
20	AA Sequence
2	Application
8	Cloned(Commentary)
8	Cofactor
2	Crystallization (Commentary)
5	Expression
12	General Information
75	Inhibitors
14	kcat/KM [mM/s]
46	Ki Value [mM]
31	KM Value [mM]
11	Localization
1	Metals/Ions
1	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
25	Organism
4	Pathway
3	PDB ID
9	pH Optimum
1	pH Stability
4	Posttranslational Modification
6	Protein Variants
7	Purification (Commentary)
1	Reaction
23	Reference
15	Source Tissue
1	Specific Activity [micromol/min/mg]
45	Substrates and Products (Substrate)
2	Subunits
22	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Stability [°C]
28	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Crystallization on EC 1.5.3.14 - polyamine oxidase (propane-1,3-diamine-forming)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

O64411

695161

purified recombinant mutant ZmPAO-K300M, hanging drop vapor diffusion method, mixing of 9.0 mg/ml protein in 50 mM sodium acetate, pH 5.5, with an equal volume of reservoir solution containing ammonium sulfate in a concentration range 2.2–2.8 m and 100 mm sodium acetate, pH 4.6, 20°C, two weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution,mlecular displacement, modelling

Zea mays

-

724968