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Literature summary extracted from

  • Adachi, M.; Taylor, A.; Hart, P.; Fitzpatrick, P.
    Mechanistic and structural analyses of the role of His67 in the yeast polyamine oxidase Fms1 (2012), Biochemistry, 51, 4888-4897.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.17 recombinant expression of His-tagged wild-type and mutant enzymes Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.3.17 purified recombinant enzyme mutant H67Q, sitting drop vapor diffusion method, mixing of protein solution, in 25 mM HEPES, pH 7.5, in a 1:1 ratio with buffer containing 20% w/v PEG 3350, 0.2 M sodium acetate, and 0.1 M bis-Tris propane, pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.5.3.17 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 Saccharomyces cerevisiae
1.5.3.17 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 Saccharomyces cerevisiae
1.5.3.17 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 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.17 additional information
-
 additional information seady-state kinetics and rapid-reaction kinetics of wild-type and mutant enzymes, overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.3.17 additional information Saccharomyces cerevisiae flavoprotein oxidase Fms1 catalyzes the oxidation of spermine and N1-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal ?
-
 ?
1.5.3.17 N1-acetylspermine + O2 + H2O Saccharomyces cerevisiae
-
 spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
1.5.3.17 spermine + O2 + H2O Saccharomyces cerevisiae
-
 spermidine + 3-aminopropanal + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.17 Saccharomyces cerevisiae P50264
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.3.17 recombinant His-tagged wild-type and mutant enzymes by nickel affinity chhromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.17 additional information flavoprotein oxidase Fms1 catalyzes the oxidation of spermine and N1-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal Saccharomyces cerevisiae ?
-
 ?
1.5.3.17 N1-acetylspermine + O2 + H2O
-
 Saccharomyces cerevisiae spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
1.5.3.17 spermine + O2 + H2O
-
 Saccharomyces cerevisiae spermidine + 3-aminopropanal + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.3.17 Fms1
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.3.17 25
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.3.17 9
-
 substrate N1-acetylspermine Saccharomyces cerevisiae
1.5.3.17 9.35
-
 substrate spermine Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.5.3.17 additional information
-
 pH profile for the reductive half-reaction of Fms1, a moiety with a pKa value of 7.2-8.3 must be unprotonated for amine oxidation, overview Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.17 FAD dependent on Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
1.5.3.17 additional information the overall catalytic reactions of flavoprotein oxidases such as Fms1 can be divided into reductive and oxidative half-reactions. In the reductive half-reaction, binding of the oxidized substrate is followed by transfer of a hydride equivalent to the flavin to form reduced flavin and oxidized substrate. In the oxidative half-reaction, the reduced flavin is oxidized by molecular oxygen to form H2O2, the oxidized amine then dissociates from the enzyme. A moiety with a pKa value of 7.2-8.3 must be unprotonated for amine oxidation Saccharomyces cerevisiae