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Literature summary extracted from

  • Cervelli, M.; Leonetti, A.; Cervoni, L.; Ohkubo, S.; Xhani, M.; Stano, P.; Federico, R.; Polticelli, F.; Mariottini, P.; Agostinelli, E.
    Stability of spermine oxidase to thermal and chemical denaturation comparison with bovine serum amine oxidase (2016), Amino Acids, 48, 2283-2291 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.16 expressed in Escherichia coli BL21 DE3 Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
1.5.3.16 additional information a mutant enzyme deprived of all but two cysteine residues (C263/C429) results in a monomeric enzyme species. The mutant enzyme is less stable than the wild type. Is activity decreased by about 90% after 1 day from the preparation, and storage at 6°C or -20°C Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.16 0.02
-
 spermine mutant enzyme deprived of all but two cysteine residues (C263/C429), pH 8.3, 25°C Mus musculus
1.5.3.16 0.09
-
 spermine wild-type enzyme, pH 8.3, 25°C Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.16 Mus musculus Q99K82
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.3.16
-
 Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Storage Stability

EC Number Storage Stability Organism
1.5.3.16 -20°C, activity decreased by about 90% after 1 day, mutant enzyme deprived of all but two cysteine residues (C263/C429) Mus musculus
1.5.3.16 6°C, activity decreased by about 90% after 1 day, mutant enzyme deprived of all but two cysteine residues (C263/C429) Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.16 spermine + O2 + H2O
-
 Mus musculus spermidine + 3-aminopropanal + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.3.16 dimer homodimeric and monomeric enzyme forms are catalytically active Mus musculus
1.5.3.16 monomer homodimeric and monomeric enzyme forms are catalytically active. A mutant enzyme deprived of all but two cysteine residues (C263/C429) results in a monomeric enzyme species Mus musculus

Synonyms

EC Number Synonyms Comment Organism
1.5.3.16 SMOX
-
 Mus musculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.3.16 62.8
-
 Tm-value Mus musculus
1.5.3.16 100
-
 thermal denaturation is irreversible after heating to 100°C Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.3.16 0.32
-
 spermine mutant enzyme deprived of all but two cysteine residues (C263/C429), pH 8.3, 25°C Mus musculus
1.5.3.16 3.5
-
 spermine wild-type enzyme, pH 8.3, 25°C Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.16 FAD
-
 Mus musculus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.3.16 16
-
 spermine mutant enzyme deprived of all but two cysteine residues (C263/C429), pH 8.3, 25°C Mus musculus
1.5.3.16 50
-
 spermine wild-type enzyme, pH 8.3, 25°C Mus musculus