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Literature summary extracted from

  • Yoshida, N.; Akazawa, S.I.; Katsuragi, T.; Tani, Y.
    Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe (2004), J. Biosci. Bioeng., 97, 278-280.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.7 DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109 Schizosaccharomyces pombe
1.5.3.18
-
 Schizosaccharomyces pombe

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.7 3 3.5 L-proline pH 8.0, 30°C, recombinant enzyme Schizosaccharomyces pombe
1.5.3.7 4.07
-
 L-pipecolate pH 8.0, 30°C, recombinant enzyme Schizosaccharomyces pombe
1.5.3.18 9.02
-
 L-saccharopine pH 8.0, 30°C Schizosaccharomyces pombe

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.3.7 56000
-
 2 * 56000, about, recombinant enzyme, SDS-PAGE Schizosaccharomyces pombe
1.5.3.7 98000
-
 recombinant enzyme, gel filtration Schizosaccharomyces pombe
1.5.3.18 49000
-
 1 * 49000, SDS-PAGE Schizosaccharomyces pombe
1.5.3.18 56000
-
 gel filtration Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.3.7 additional information Schizosaccharomyces pombe enzyme is involved in L-lysine metabolism ?
-
 ?
1.5.3.18 L-saccharopine + H2O + O2 Schizosaccharomyces pombe Fap2 may play a role in L-lysine metabolism when a large amount of L-saccharopine is accumulated L-2-aminoadipate 6-semialdehyde + L-glutamate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.7 Schizosaccharomyces pombe
-
 gene FAP1
-
1.5.3.18 Schizosaccharomyces pombe Q9UTM9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.3.7 recombinant enzyme from Escherichia coli strain JM109 Schizosaccharomyces pombe

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.3.7 additional information
-
-
 Schizosaccharomyces pombe
1.5.3.18 6.72
-
 pH 8.0, 30°C Schizosaccharomyces pombe

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.7 L-pipecolate + O2 highly specific for Schizosaccharomyces pombe 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
-
 ?
1.5.3.7 L-proline + O2 low activity Schizosaccharomyces pombe ?
-
 ?
1.5.3.7 additional information enzyme is involved in L-lysine metabolism Schizosaccharomyces pombe ?
-
 ?
1.5.3.7 additional information no activity with fructosyl-amino acids, L-saccharopine, and sarcosine Schizosaccharomyces pombe ?
-
 ?
1.5.3.18 L-saccharopine + H2O + O2
-
 Schizosaccharomyces pombe L-2-aminoadipate 6-semialdehyde + L-glutamate + H2O2
-
 ?
1.5.3.18 L-saccharopine + H2O + O2 Fap2 may play a role in L-lysine metabolism when a large amount of L-saccharopine is accumulated Schizosaccharomyces pombe L-2-aminoadipate 6-semialdehyde + L-glutamate + H2O2
-
 ?
1.5.3.18 additional information no activity with L-pipecolate, sarcosine, L-proline, Nepsilon-fructosyl Nalpha-Z-lysine or fructosyl valine Schizosaccharomyces pombe ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.3.7 dimer 2 * 56000, about, recombinant enzyme, SDS-PAGE Schizosaccharomyces pombe
1.5.3.18 monomer 1 * 49000, SDS-PAGE Schizosaccharomyces pombe

Synonyms

EC Number Synonyms Comment Organism
1.5.3.7 Fap1
-
 Schizosaccharomyces pombe
1.5.3.18 FAP2
-
 Schizosaccharomyces pombe

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.3.7 30
-
 assay at Schizosaccharomyces pombe

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.3.7 8
-
 assay at Schizosaccharomyces pombe

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.7 FAD covalently attached Schizosaccharomyces pombe
1.5.3.18 FAD covalently linked to the protein molecule Schizosaccharomyces pombe