Get Copper amine oxidases : structures, catalytic mechanisms, PDF

By Giovanni Floris, Bruno Mondovi

ISBN-10: 1420076809

ISBN-13: 9781420076806

Although the volume of analysis on copper amine oxidases has grown swiftly and considerably some time past decade, the sphere regrettably suffers from loss of unity and critical confusion surrounds features so simple as affirmation of enzyme identities. This publication 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 diversities of among AOs from micro organism, vegetation, and mammals. ultimately, 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

Example text

The dialysis against the KCN-containing buffer solution was carried out three times under dinitrogen atmosphere. , 1997 and 1998). 2). Added to the solution was solid potassium cyanide (final concentration of 10 mM). 0 mM and dialysis was continued for 3 to 24 hr, followed by final dialysis against three buffer changes. , 1994a). The solution previously de-aerated by dinitrogen was kept at minimum flow during dialysis. A brown precipitate of Cu(II)– DDC was removed by centrifugation. Excess DDC, sulfide, and dithionite were removed by dialysis.

22, diamine oxidase. 21 New entry Accepted name: primary amine oxidase. Reaction: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2. Other name(s): amine oxidase; amine oxidase (copper-containing); benzylamine oxidase; copper amine oxidase; Cu-amine oxidase; semicarbazide-sensitive amine oxidase; SSAO; polyamine oxidase; amine oxidase (pyridoxal containing; diamine oxidase; diamino oxhydrase; monoamine oxidase; histamine deaminase; histamine oxidase; plasma monoamine oxidase. Systematic name: primary amine:oxygen oxidoreductase (deaminating and copper-containing).

However, the reason for the difference observed in these AOs is unclear. , 1981). The anaerobic incubation of Cu-depleted BSAO with Co(II) produced a colored solution. The pink color of Co(II) BSAO results from an intense absorption band at 470 nm, which is similar to that of native BSAO. The MCD spectrum displaying a small positive band around 480 nm and negative band around 580 nm suggests that the high-spin Co(II) site having a tetrahedral geometry is located in BSAO. The CD peaks at 370 and 440 nm can be assigned to TPQox and that around 540 nm is due to the d–d transitions of Co(II).

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Copper amine oxidases : structures, catalytic mechanisms, and role in pathophysiology by Giovanni Floris, Bruno Mondovi


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