2005•European Journal of Inorganic ChemistryRequires access

Catalytic Properties and the Role of Copper in Bovine and Lentil Seedling Copper/Quinone‐Containing Amine Oxidases: Controversial Opinions

Enzo Agostinelli, Francesca Belli, Laura Dalla Vedova, Silvia Longu, Anna Mura, Giovanni Floris

Open publisher page 17 citations

Abstract

Abstract 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)

About this research paper

What this paper is about

Abstract 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)

Why it matters

OpenAlex reports 17 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Abstract 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)

Key concepts: Chemistry, Amine oxidase, Quinone, Copper, Enzyme, Amine gas treating, Catalysis, Cofactor

Related papers

Back to paper searchBrowse research topicsOriginal source
Catalytic Properties and the Role of Copper in Bovine and Lentil Seedling Copper/Quinone‐Containing Amine Oxidases: Controversial Opinions — Research Paper | ScholarLens