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Literature summary for 1.4.3.21 extracted from

  • Di Paolo, M.L.; Pesce, C.; Lunelli, M.; Scarpa, M.; Rigo, A.
    N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: a kinetic and spectroscopic study (2007), Arch. Biochem. Biophys., 465, 50-60.
    View publication on PubMed
Search for more literature for 1.4.3.21

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-aminobutane + H2O + O2
-
 Bos taurus butanal + NH3 + H2O2
-
 ?
1-aminoheptane + H2O + O2
-
 Bos taurus heptanal + NH3 + H2O2
-
 ?
1-aminohexane + H2O + O2
-
 Bos taurus hexanal + NH3 + H2O2
-
 ?
1-aminononane + H2O + O2 the aliphatic chain of 1-aminononane induces a shift in the pKa-value of the product Schiff base, the hydrolysis of which appears to be a rate-determining step of the reaction Bos taurus nonanal + NH3 + H2O2
-
 ?
1-aminooctane + H2O + O2
-
 Bos taurus octanal + NH3 + H2O2
-
 ?
1-aminopentane + H2O + O2
-
 Bos taurus pentanal + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
bovine serum amine oxidase
-
 Bos taurus
BSAO
-
 Bos taurus