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Literature summary extracted from

  • Peter, C.; Laliberte, J.; Beaudoin, J.; Labbe, S.
    Copper distributed by Atx1 is available to copper amine oxidase 1 in Schizosaccharomyces pombe (2008), Eukaryot. Cell, 7, 1781-1794.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.3.21 Atx1-like protein required for the synthesis of fully active Cao1 Schizosaccharomyces pombe
1.4.3.21 additional information active Cao1 requires Ctr4/5-mediated copper transport and the transcription factor Cuf1 Schizosaccharomyces pombe

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.21 genes cao1+ and cao2+, cDNA library screening, DNA and amino acid determination and analysis, both genes are expressed in wild-type cells, but only the expression of cao1+,not of cao2+, results in production of an active enzyme. Expression of cao1+ and cao2+ is copper-independent and is not regulated by Cuf1. Recombinant expression of GFP-tagged Cao1 in the cytosol, expression of wild-type and mutant enzymes in Saccharomyces cerevisiae Schizosaccharomyces pombe

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.21 H456A site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme Schizosaccharomyces pombe
1.4.3.21 H458A site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme Schizosaccharomyces pombe
1.4.3.21 H460A site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme Schizosaccharomyces pombe
1.4.3.21 H621A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Schizosaccharomyces pombe
1.4.3.21 H627A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Schizosaccharomyces pombe

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.21 Cu2+ absolutely required for catalytic activity Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.21 ethylamine + H2O + O2 Schizosaccharomyces pombe
-
 acetaldehyde + NH3 + H2O2
-
 ?
1.4.3.21 ethylamine + H2O + O2 Schizosaccharomyces pombe FY435 / ATCC 87284
-
 acetaldehyde + NH3 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 no activity in Saccharomyces cerevisiae
-
-
-
1.4.3.21 Schizosaccharomyces pombe
-
 gene cao1+
-
1.4.3.21 Schizosaccharomyces pombe FY435 / ATCC 87284
-
 gene cao1+
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 ethylamine + H2O + O2
-
 Schizosaccharomyces pombe acetaldehyde + NH3 + H2O2
-
 ?
1.4.3.21 ethylamine + H2O + O2
-
 Schizosaccharomyces pombe FY435 / ATCC 87284 acetaldehyde + NH3 + H2O2
-
 ?
1.4.3.21 additional information three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity Schizosaccharomyces pombe ?
-
 ?
1.4.3.21 additional information three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity Schizosaccharomyces pombe FY435 / ATCC 87284 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.21 dimer
-
 Schizosaccharomyces pombe

Synonyms

EC Number Synonyms Comment Organism
1.4.3.21 CAO
-
 Schizosaccharomyces pombe
1.4.3.21 Copper amine oxidase
-
 Schizosaccharomyces pombe
1.4.3.21 copper amine oxidase 1
-
 Schizosaccharomyces pombe

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.21 37
-
 assay at Schizosaccharomyces pombe

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.21 7.4
-
 assay at Schizosaccharomyces pombe

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.21 2,4,5-trihydroxyphenylalanine quinone i.e. TPQ, covalently bound cofactor, one per monomer, generated by posttranslational modification of the first conserved tyrosine residue in the consensus sequence Asn-Tyr-(Glu/Asp)-Tyr Schizosaccharomyces pombe

General Information

EC Number General Information Comment Organism
1.4.3.21 physiological function Cao1 may enable Schizosaccharomyces pombe cells to utilize primary amines as sources of nitrogen Schizosaccharomyces pombe