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Literature summary extracted from

  • Tavladoraki, P.; Cervelli, M.; Antonangeli, F.; Minervini, G.; Stano, P.; Federico, R.; Mariottini, P.; Polticelli, F.
    Probing mammalian spermine oxidase enzyme-substrate complex through molecular modeling, site-directed mutagenesis and biochemical characterization (2011), Amino Acids, 40, 1115-1126.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.16 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.3.16 molecular modeling of enzyme and enzyme-spermine complex. Spermine oxidase binds spermine in a similar conformation as that observed in the yeast polyamine oxidase FMS1-spermine complex, with a major role for residues H82 and K367 in substrate binding and catalysis. The enzyme–substrate complex shows an active site pocket with highly polar characteristics Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
1.5.3.16 H82E no catalytic activity Mus musculus
1.5.3.16 H82E site-directed mutagenesis, inactive mutant Mus musculus
1.5.3.16 H82Q site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Mus musculus
1.5.3.16 H82Q about 300fold decrease in catalytic efficiency Mus musculus
1.5.3.16 K367M site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Mus musculus
1.5.3.16 K367M about 3fold decrease in catalytic efficiency Mus musculus
1.5.3.16 additional information wild-type and mutant proteins share essentially the same structural properties. The pH-dependency of the catalytic activity of H82Q is essentially unchanged with respect to the wild-type, while a slight shift toward higher pH values is observed for the K367M mutant Mus musculus
1.5.3.16 T428Y no catalytic activity Mus musculus
1.5.3.16 T528Y site-directed mutagenesis, inactive mutant Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.3.16 N1,N4-bis(2,3-butadienyl)-1,4-butanediamine i.e. MDL72527, inhibits FAD-containing polyamine oxidases Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.16 0.021
-
 spermine mutant K367M, pH 8.5, 25°C Mus musculus
1.5.3.16 0.021
-
 spermine pH 8.5, 25°C, recombinant mutant K367M Mus musculus
1.5.3.16 0.242
-
 spermine wild-type, pH 8.5, 25°C Mus musculus
1.5.3.16 0.242
-
 spermine pH 8.5, 25°C, recombinant wild-type enzyme Mus musculus
1.5.3.16 0.53
-
 spermine mutant H82Q, pH 8.5, 25°C Mus musculus
1.5.3.16 0.53
-
 spermine pH 8.5, 25°C, recombinant mutant H82Q Mus musculus

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.3.16 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography 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
-
 ?
1.5.3.16 spermine + O2 + H2O SMO oxidizes the carbon on the exo side of the N5-nitrogen of SPM producing spermidine, 3-aminopropanal, and H2O2 Mus musculus spermidine + 3-aminopropanal + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.3.16 SMO
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.3.16 25
-
 assay at 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 0.024
-
 spermine mutant H82Q, pH 8.5, 25°C Mus musculus
1.5.3.16 0.024
-
 spermine pH 8.5, 25°C, recombinant mutant H82Q Mus musculus
1.5.3.16 0.1
-
 spermine mutant K367M, pH 8.5, 25°C Mus musculus
1.5.3.16 0.1
-
 spermine pH 8.5, 25°C, recombinant mutant K367M Mus musculus
1.5.3.16 3.57
-
 spermine wild-type, pH 8.5, 25°C Mus musculus
1.5.3.16 3.57
-
 spermine pH 8.5, 25°C, recombinant wild-type enzyme Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.3.16 8.5
-
 assay at Mus musculus
1.5.3.16 8.5
-
 wild-type and mutant H82Q Mus musculus
1.5.3.16 9 9.5 mutant K367M Mus musculus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.5.3.16 6.5 8.5 recombinant wild-type MmSMO enzymatic activity increases in the pH range, reaching a maximum at pH 8.5 and decreasing for higher pH values Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.16 FAD dependent on Mus musculus

General Information

EC Number General Information Comment Organism
1.5.3.16 additional information substrate binding and catalytic mechanism, spermine docking into the active site, CD spectroscopy, structure modelling, overview 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 0.00000005
-
 spermine pH 8.5, 25°C, recombinant mutant H82Q Mus musculus
1.5.3.16 0.000005
-
 spermine pH 8.5, 25°C, recombinant mutant K367M Mus musculus
1.5.3.16 0.000015
-
 spermine pH 8.5, 25°C, recombinant wild-type enzyme Mus musculus
1.5.3.16 0.00005
-
 spermine mutant H82Q, pH 8.5, 25°C Mus musculus
1.5.3.16 0.0015
-
 spermine wild-type, pH 8.5, 25°C Mus musculus
1.5.3.16 0.005
-
 spermine mutant K367M, pH 8.5, 25°C Mus musculus