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Literature summary for 1.5.3.14 extracted from

  • Cona, A.; Manetti, F.; Leone, R.; Corelli, F.; Tavladoraki, P.; Polticelli, F.; Botta, M.
    Molecular basis for the binding of competitive inhibitors of maize polyamine oxidase (2004), Biochemistry, 43, 3426-3435.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-Diaminodecane
-
Zea mays
1,12-diaminododecane
-
Zea mays
1,3-diaminopropane
-
Zea mays
1,4-diaminobutane
-
Zea mays
1,5-Diaminopentane
-
Zea mays
1,6-diaminohexane
-
Zea mays
1,7-Diaminoheptane
-
Zea mays
1,8-diaminooctane
-
Zea mays
1,9-diaminononane
-
Zea mays
additional information docking simulations carried out with the charged and uncharged forms of MPAO inhibitors indicate that the stereoelectronic properties of the MPAO active site are consistent with the binding of inhibitors in the protonated form, a feature which can shed light on the still obscure MPAO catalytic mechanism Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays O64411
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
spermidine + O2 + H2O
-
Zea mays ?
-
?

Synonyms

Synonyms Comment Organism
MPAO
-
Zea mays

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00017
-
1,12-diaminododecane pH 6.0, 25°C Zea mays
0.0003
-
1,8-diaminooctane pH 6.0, 25°C Zea mays
0.0004
-
1,7-Diaminoheptane pH 6.0, 25°C Zea mays
0.0006
-
1,10-Diaminodecane pH 6.0, 25°C Zea mays
0.0012
-
1,9-diaminononane pH 6.0, 25°C Zea mays
0.003
-
1,6-diaminohexane pH 6.0, 25°C Zea mays
0.038
-
1,5-Diaminopentane pH 6.0, 25°C Zea mays
0.1
-
1,3-diaminopropane pH 6.0, 25°C Zea mays
0.13
-
1,4-diaminobutane pH 6.0, 25°C Zea mays