Copper amine oxidases : structures, catalytic mechanisms, by Giovanni Floris, Bruno Mondovi

By Giovanni Floris, Bruno Mondovi

Although the quantity of analysis on copper amine oxidases has grown swiftly and considerably some time past decade, the sphere regrettably suffers from loss of harmony and important confusion surrounds points so simple as affirmation of enzyme identities. This publication describes the constitution of the enzymes, the function of copper, and of the weird cofactor 6-hydroxydopa quinine derived from a posttranslational amendment of a tyrosine residue. It additionally covers the diversities of among AOs from micro organism, crops, and mammals. eventually, the textual content examines the significance of this ubiquitous type of enzymes in body structure and in metabolism of biogenic amines.

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Additional info for Copper amine oxidases : structures, catalytic mechanisms, and role in pathophysiology

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TPQsq = semiquinone form of TPQ. TPQimq = iminoquinone form of TPQ. The reductive and oxidative half-reactions are shown in solid and dotted boxes, respectively. 4 Structures of TPQ cofactor and model compounds. 1995). The broad absorbance around 480 nm of CAO arises from the resonance stabilized mono-anion form of TPQ. The λmax of this absorption varies from 450 to 500 nm at physiological pH, depending on the origin of CAO and the effects of mutations in the active site. Solution chemistry suggests an explanation for this observed variation as the λmax of the resonance stabilized mono-anionic TPQ is solvent-dependent (Mure and Klinman 1995a).

1 Proposed reaction mechanisms of CAOs. TPQox = resting (oxidized) form of TPQ. SSB = substrate Schiff base intermediate. PSB = product Schiff base intermediate. TPQred = substrate reduced (aminoquinol) form of TPQ. TPQsq = semiquinone form of TPQ. TPQimq = iminoquinone form of TPQ. The reductive and oxidative half-reactions are shown in solid and dotted boxes, respectively. 4 Structures of TPQ cofactor and model compounds. 1995). The broad absorbance around 480 nm of CAO arises from the resonance stabilized mono-anion form of TPQ.

2). 7 Å)). The Cu(II)-to-Wat2 distance longer than the Cu(II)-to-Wat1 distance is explained by the Jahn–Teller effect. 3 Å). , 2003). This orientation of the TPQ ring is identical with those in the active forms of E. 7 Å). A structural comparison of the active sites of these three enzymes shows that TPQox in Co(II) and Ni(II) AGAOs is held in a conformation similar to the TPQox cofactor in native AGAO. 2 Metal coordination structures of (a) Cu(II) AGAO, (b) Co(II) AGAO, and (c) Ni(II) AGAO. PDB accession codes: Cu (1IU7), Co (1IQX), and Ni (1IQY).

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