TAILIEUCHUNG - Báo cáo khoa học: An important lysine residue in copper⁄quinone-containing amine oxidases

The interaction of xenon with copper⁄6-hydroxydopa (2,4,5-trihydroxy-phenethylamine) quinone (TPQ) amine oxidases from the plant pulses lentil (Lens esculenta) and pea (Pisum sativum) (seedlings), the perennial Mediter-ranean shrub Euphorbia characias(latex), and the mammals cattle (serum) and pigs (kidney), were investigated by NMR and optical spectroscopy of the aqueous solutions of the enzymes. | ỊFEBS Journal An important lysine residue in copper quinone-containing amine oxidases Anna Mura1 Roberto Anedda2 Francesca Pintus1 Mariano Casu2 Alessandra Padiglia1 Giovanni Floris1 and Rosaria Medda1 1 Department of Applied Sciences in Biosystems University of Cagliari Italy 2 Department of ChemicalScience University of Cagliari Italy Keywords amine oxidase copper NMR quinoprotein xenon Correspondence R. Medda Department of Applied Sciences in Biosystems University of Cagliari Cittadella Universitaria I-09042 Monserrato CA Italy Fax 39 070 6754524 Tel 39 070 6754517 E-mail rmedda@ Received 4 October 2006 revised 27 February 2007 accepted 15 March 2007 doi The interaction of xenon with copper 6-hydroxydopa 2 4 5-trihydroxy-phenethylamine quinone TPQ amine oxidases from the plant pulses lentil Lens esculenta and pea Pisum sativum seedlings the perennial Mediterranean shrub Euphorbia characias latex and the mammals cattle serum and pigs kidney were investigated by NMR and optical spectroscopy of the aqueous solutions of the enzymes. 129Xe chemical shift provided evidence of xenon binding to one or more cavities of all these enzymes and optical spectroscopy showed that under 10 atm of xenon gas and in the absence of a substrate the plant enzyme cofactor TPQ is converted into its reduced semiquinolamine radical. The kinetic parameters of the analyzed plant amine oxidases showed that the kc value of the xenon-treated enzymes was reduced by 40 . Moreover whereas the measured Km value for oxygen and for the aromatic monoamine benzylamine was shown to be unchanged the Km value for the diamine putrescine increased remarkably after the addition of xenon. Under the same experimental conditions the TPQ of bovine serum amine oxidase maintained its oxidized form whereas in pig kidney the reduced aminoquinol species was formed without the radical species. Moreover the kc value of the xenon-treated pig enzyme in the presence of both .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• molecular Biology
• tumor cells
• Antimicrobial
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• biochemical studies
• environmental medicine