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Download Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology djvu

Download Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology djvu

by Giovanni Floris,Bruno Mondovi

Author: Giovanni Floris,Bruno Mondovi
Subcategory: Medicine & Health Sciences
Language: English
Publisher: CRC Press; 1 edition (June 1, 2009)
Pages: 374 pages
Category: Other
Rating: 4.2
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Copper amine oxidases (CAOs) catalyse the oxidation of various aliphatic amines to the corresponding aldehydes, ammonia and hydrogen peroxide.

Copper amine oxidases (CAOs) catalyse the oxidation of various aliphatic amines to the corresponding aldehydes, ammonia and hydrogen peroxide. With BHZ and 4-OH-BHZ, but not with PHZ, the inhibitor aromatic ring is bound to a hydrophobic cavity near the active site in a well-defined conformation. Furthermore, the hydrogen atom on the hydrazone nitrogen is located closer to the catalytic base in the BHZ and 4-OH-BHZ adducts than in the PHZ adduct.

Floris, G. (E., Mondovi, B. Copper Amine Oxidases

Floris, G. Copper Amine Oxidases. This book describes the structure of the enzymes, the role of copper, and of the unusual co. Table of contents.

Copper Amine Oxidases from Plants, R. Medda, A. Bellelli, P. Pec, R. Federico, . ona, and G. Floris. Soluble Copper Amine Oxidases from Mammals, P. Pietrangeli, L. Morpurgo, B. Mondovi, M. L. Di Paolo, and A. Rigo. Membrane-Bound Copper Amine Oxidases, A. Holt. Copper Amine Oxidase Genes, I. Frebort and H. G. Schwelberger. Mechanism of TPQ Biogenesis in Prokaryotic Copper Amine Oxidase, T. Okajima and . anizawa. Copper Amine Oxidase Crystal Structures, J. Mitchell Guss, G. Zanotti, and T. A. Salminen.

Copper Amine Oxidases book. Goodreads helps you keep track of books you want to read

Copper Amine Oxidases book. Goodreads helps you keep track of books you want to read. Start by marking Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology as Want to Read: Want to Read savin. ant to Read.

This book describes the structure of the enzymes, the role of copper, and of the unusual cofactor 6-hydroxydopa quinine derived from a posttranslational modification of a tyrosine residue. It also covers the differences of between AOs from bacteria, plants, and mammals

This book describes the structure of the enzymes, the role of copper, and of the unusual cofactor 6-hydroxydopa quinine derived from a posttranslational modification of a tyrosine residue. It also covers the differences of between AOs from bacteria, plants, and mammals

Giovanni Floris, Bruno Mondovi.

Giovanni Floris, Bruno Mondovi. This book describes the structure of the enzymes, the role of copper, and of the unusual cofactor 6-hydroxydopa quinine derived from a posttranslational modification of a tyrosine residue. It also covers the differences of between AOs from bacteria, plants, and mammals. It also covers the differences of between AOs from bacteria, plants, and mammals

Amine oxidases (AOs) are a class of enzymes which are heterogeneous in terms of structure . Floris G, Mondovì B (eds) (2009) Copper amine oxidases: structures, catalytic mechanisms, and role in pathophysiology.

Amine oxidases (AOs) are a class of enzymes which are heterogeneous in terms of structure, catalytic mechanisms, and substrate specificity. Biogenic amines, mono, di, and polyamines as well as N-acetyl amines, are oxidatively deaminated by AOs in a reaction that consumes O2 to produce the corresponding aldehydes, amines with a shorter chain, ammonium ions, and hydrogen peroxide (H2O2). CRC Press/Taylor & Francis Group, Boca RatonGoogle Scholar.

Although the amount of research on copper amine oxidases has grown rapidly and substantially in the past decade, the field unfortunately suffers from lack of cohesion and significant confusion surrounds aspects as simple as confirmation of enzyme identities. This book describes the structure of the enzymes, the role of copper, and of the unusual cofactor 6-hydroxydopa quinine derived from a posttranslational modification of a tyrosine residue. It also covers the differences of between AOs from bacteria, plants, and mammals. Finally, the text examines the importance of this ubiquitous class of enzymes in physiology and in metabolism of biogenic amines.