Literature summary for 1.4.3.21 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.

Activating Compound

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

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Subunits	Comment	Organism
dimer	-	Schizosaccharomyces pombe

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
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

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