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1.5.3.17: non-specific polyamine oxidase

This is an abbreviated version!
For detailed information about non-specific polyamine oxidase, go to the full flat file.

Word Map on EC 1.5.3.17

Reaction

N1-acetylspermidine
+
O2
 +
H2O
=
putrescine
 +
3-acetamidopropanal
 +
H2O2

Synonyms

AtPAO2, AtPAO3, AtPAO4, AtPAO5, Bjpao1, Bjpao2, EC 1.5.3.11, Fms1, LC036642, OsPAO1, PAO, PAO1, PAO2, PAO3, PAO5, polyamine oxidase 1, SelPAO5, slr5093, T-Spm oxidase, thermospermine oxidase

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.3 With oxygen as acceptor
                1.5.3.17 non-specific polyamine oxidase

Engineering

Engineering on EC 1.5.3.17 - non-specific polyamine oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H64E
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
H64Q
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
H69E
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
H69Q
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
K301M
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
K315M
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
T460S
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
T460Y
Vmax values for mutant enzyme with substrate spermine or spermidine are lower than Vmax values for wild-type enzym. Km values for mutant enzyme with substrate spermine or spermidine are higher than Km values for wild-type enzym
T467S
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
T467Y
compared with the wild-type enzyme the mutant enzyme shows lower Vmax values and higher Km-values for the substrates spermidine and N1-acetylspermine
H64A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H64N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H64Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D94N
site-directed mutagenesis, the mutation primarily affects the reductive half-reaction. The mutant shows 20-40fold reduced rate constant for flavin reduction with spermine and 450fold with N1-acetylspermine compared to the wild-type enzyme
H67A
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
H67N
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
H67Q
site-directed mutagenesis, the mutant shows a 2-3fold reduced first-order rate constant for flavin reduction and slightly altered kinetics compared to the wild-type enzyme
N195A
site-directed mutagenesis, the mutation primarily affects the reductive half-reaction. The mutant shows 20-40fold reduced rate constant for flavin reduction with spermine and 450fold with N1-acetylspermine compared to the wild-type enzyme. Mutant N195A enzyme shows structure with a molecule of tetraethylene glycol in the active site, the mutation has no effect on the protein structure
additional information