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Catalytic Properties and the Role of Copper in Bovine and Lentil Seedling Copper/Quinone‐Containing Amine Oxidases: Controversial Opinions
Author(s) -
Agostinelli Enzo,
Belli Francesca,
Dalla Vedova Laura,
Longu Silvia,
Mura Anna,
Floris Giovanni
Publication year - 2005
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.200401020
Subject(s) - chemistry , amine oxidase , quinone , copper , enzyme , amine gas treating , catalysis , cofactor , amine oxidase (copper containing) , catalytic cycle , biochemistry , organic chemistry , diamine oxidase
In this microreview, the differences in the catalytic cycle of two copper/quinone‐containing amine oxidases, one from lentil seedlings, representative of plant enzymes, and the other from bovine serum, typical of mammalian enzymes, are discussed. Although both enzymes are involved in the control of the levels of mono‐, di‐, and polyamines, and contain the same organic cofactor, the quinone of 2,4,5‐trihydroxyphenylalanine, known as TOPA or TPQ, lentil amine oxidase operates in a different way and with a much higher catalytic activity than the bovine serum enzyme. The role of copper in the two enzymes is also discussed. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)