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Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group
Author(s) -
Lobenstein-Verbeek C.L.,
Jongejan J.A.,
Frank J.,
Duine J.A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81333-2
Subject(s) - amine oxidase , covalent bond , enzyme , chemistry , biochemistry , amine gas treating , lysyl oxidase , cofactor , organic chemistry
In addition to the metal ion, copper‐containing amine oxidases possess an organic prosthetic group, the nature of which has long been controversial. We show here that in the case of bovine plasma amine oxidase, this second prosthetic group is covalently bound pyrroloquinoline quinone (PQQ). Until now the coenzyme PQQ has been found in several bacterial dehydrogenases. Thus the finding reported here is the first example of a quinoprotein oxidoreductase discovered in a eukaryotic organism.