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Literature summary for 1.5.3.14 extracted from

  • Polticelli, F.; Basran, J.; Faso, C.; Cona, A.; Minervini, G.; Angelini, R.; Federico, R.; Scrutton, N.S.; Tavladoraki, P.
    Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase (2005), Biochemistry, 44, 16108-16120.
    View publication on PubMed
Search for more literature for 1.5.3.14

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris, wild-type and mutant enzymes Zea mays

Protein Variants

Protein Variants Comment Organism
E170Q mutation results in moderate change of enzyme activity and apparent Km-values Zea mays
E62Q mutation results in moderate change of enzyme activity and apparent Km-values Zea mays
K300M mutation results in a 1400fold decrease in the rate of flavin reduction and a 160fold decrease in the equilibrium dissociation constant for the K300M-spermidine complex, consistent with a major role for this residue in the mechanism of substrate oxidation Zea mays
Y298F specific activity or KM-values are not substantially altered Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0007
-
 spermidine pH 6.0, 25°C, mutant enzyme Y298F Zea mays
0.0012
-
 spermine pH 6.0, 25°C, mutant enzyme Y298F Zea mays
0.0016
-
 spermine pH 6.0, 25°C, wild-type enzyme Zea mays
0.0017
-
 spermidine pH 6.0, 25°C, native enzyme Zea mays
0.0017
-
 spermine pH 6.0, 25°C, native enzyme Zea mays
0.0021
-
 spermidine pH 6.0, 25°C, wild-type enzyme Zea mays
0.0125
-
 spermine pH 6.0, 25°C, mutant enzyme E170Q Zea mays
0.0147
-
 spermine pH 6.0, 25°C, mutant enzyme E62Q Zea mays
0.0167
-
 spermidine pH 6.0, 25°C, mutant enzyme E170Q Zea mays
0.0246
-
 spermidine pH 6.0, 25°C, mutant enzyme E62Q Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays O64411
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
 Zea mays
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
MPAO
-
 Zea mays

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.004
-
 spermidine pH 6.0, 25°C, mutant enzyme K300M Zea mays
0.0053
-
 spermine pH 6.0, 25°C, mutant enzyme K300M Zea mays
2.8
-
 spermine pH 6.0, 25°C, mutant enzyme E62Q Zea mays
4.6
-
 spermine pH 6.0, 25°C, mutant enzyme E170Q Zea mays
7.7
-
 spermine pH 6.0, 25°C, mutant enzyme Y298F Zea mays
8.3
-
 spermidine pH 6.0, 25°C, mutant enzyme E62Q Zea mays
16.5
-
 spermidine pH 6.0, 25°C, mutant enzyme Y298F Zea mays
17.3
-
 spermidine pH 6.0, 25°C, mutant enzyme E170Q Zea mays
32.9
-
 spermine pH 6.0, 25°C, wild-type enzyme Zea mays
39.3
-
 spermine pH 6.0, 25°C, native enzyme Zea mays
50.2
-
 spermidine pH 6.0, 25°C, wild-type enzyme Zea mays
55.1
-
 spermidine pH 6.0, 25°C, native enzyme Zea mays

Cofactor

Cofactor Comment Organism Structure
FAD oxidized FAD is the prominent form during steady-state turnover, consistent with the reductive half-reaction being rate-limiting Zea mays