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Literature summary for 1.5.3.17 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
Search for more literature for 1.5.3.17

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
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
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
 ?
N1-acetylspermine + O2 + H2O Saccharomyces cerevisiae
-
 spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
spermine + O2 + H2O Saccharomyces cerevisiae
-
 spermidine + 3-aminopropanal + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P50264
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
N1-acetylspermine + O2 + H2O
-
 Saccharomyces cerevisiae spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
spermine + O2 + H2O
-
 Saccharomyces cerevisiae spermidine + 3-aminopropanal + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
Fms1
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

Cofactor Comment Organism Structure
FAD dependent on Saccharomyces cerevisiae

General Information

General Information Comment Organism
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