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.
Word Map on EC 1.5.3.14
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1.5.3.14
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spermine
-
oxidases
-
back-conversion
-
apoplastic
-
thermospermine
-
putrescine
-
tabacum
-
fad-dependent
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tunnel
-
barley
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mesocotyl
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1,3-diaminopropane
-
tetraamines
-
aminoaldehyde
-
1,8-diaminooctane
-
h2o2-producing
-
u-shaped
-
guazatine
- 1.5.3.14
- spermine
- oxidases
-
back-conversion
- apoplastic
- thermospermine
- putrescine
- tabacum
-
fad-dependent
-
tunnel
- barley
- mesocotyl
- 1,3-diaminopropane
-
tetraamines
- aminoaldehyde
- 1,8-diaminooctane
-
h2o2-producing
-
u-shaped
- guazatine
Reaction
Synonyms
EC 1.5.3.11, flavin-containing polyamine oxidase, maize PAO, maize polyamine oxidase, MPAO, OsPAO7, PAO, ZmPAO
ECTree
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Cofactor
Cofactor on EC 1.5.3.14 - polyamine oxidase (propane-1,3-diamine-forming)
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FAD
oxidized FAD is the prominent form during steady-state turnover, consistent with the reductive half-reaction being rate-limiting
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
FAD
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dependent on. Residue K300 is hydrogen-bound to the N5 atom of FAD via a H2O molecule (HOH309), the only solvent molecule present inside the catalytic site in the enzyme inhibitor complexes. In turn, K300 is the only active-site residue whose conformation changes upon FAD reduction, possibly allowing for a reorientation of the HOH309 molecule. The water molecule might thus function as a hydrogen-bond acceptor with the protonated N5 atom of reduced FAD