Copper Amine Oxidases: Structures, Catalytic Mechanisms and by Giovanni Floris, Bruno Mondovi PDF

By Giovanni Floris, Bruno Mondovi

Even supposing the volume of study on copper amine oxidases has grown speedily and considerably long ago decade, the sector regrettably suffers from loss of team spirit and critical confusion surrounds features so simple as affirmation of enzyme identities. This e-book describes the constitution of the enzymes, the position of copper, and of the bizarre cofactor 6-hydroxydopa quinine derived from a posttranslational amendment of a tyrosine residue. It additionally covers the variations of among AOs from micro organism, vegetation, and mammals. eventually, the textual content examines the significance of this ubiquitous classification of enzymes in body structure and in metabolism of biogenic amines.

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Additional resources for Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology

Sample text

6 were originally distinguished as monoamine oxidase (also known as tyramine oxidase or tyraminase) and diamine oxidase (DAO, also known as histaminase). Those names were changed after the discoveries that MAO could catalyze the deamination of some diamines and that the DAO from some sources was active toward some monoamines but exhibited little activity toward histamine. Resistance to change may be the main reason for the persistence of this unsatisfactory state, but confusion on the part of both students and researchers about which results refer to what enzyme indicates it is clearly time to clarify the issue.

6; CAOs] contain a redox-active organic cofactor, 2,4,5-trihydroxyphenylalanine ­quinone (TPQ) that is essential for catalyzing the oxidation of primary amines by dioxygen to the corresponding aldehydes, ammonia, and hydrogen peroxide. 2) Each monomer of a dimeric CAO also encompasses one Cu(II) ion as an inorganic cofactor, which is electron paramagnetic resonance (EPR)-detectable non-blue (or type 2) copper (Lindley, 2001). The yellowish pink color of CAOs stems from an intense absorption band in the 460- to 500-nm region assigned to TPQox.

4d) where such an interaction is expected to be absent, amines do not attack the carbonyl carbons but instead attack the ring carbon. 4a). However, only the 2-methoxy group can support the substrate Schiff base formation in which ring amination occurs when the methoxy group is at the C3 position. 4b) with amines is much slower than that with TPQ, it still demonstrates that the hydrogen bond acceptor at C2 position (equivalent to C4 in the TPQ cofactor) is essential for Schiff base formation. TPQ is connected to the peptide backbone of CAO through the methylene group that originates from the conserved precursor Tyr residue (Y382 in AGAO).

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