TAILIEUCHUNG - Báo cáo khoa học: What’s in a covalent bond? On the role and formation of covalently bound flavin cofactors

Many enzymes use one or more cofactors, such as biotin, heme, or flavin. These cofactors may be bound to the enzyme in a noncovalent or covalent manner. Although most flavoproteins contain a noncovalently bound flavin cofactor (FMN or FAD), a large number have these cofactors covalently linked to the polypeptide chain. Most covalent flavin–protein linkages involve a single cofactor attachment via a histidyl, tyrosyl, cysteinyl or threonyl linkage. | ỊFEBS Journal REVIEW ARTICLE What s in a covalent bond On the role and formation of covalently bound flavin cofactors Dominic P. H. M. Heuts1 Nigel S. Scrutton2 William S. McIntire3 4 and Marco W. Fraaije1 1 Laboratory of Biochemistry Groningen Biomolecular Sciences and Biotechnology Institute University of Groningen The Netherlands 2 Manchester Interdisciplinary Biocentre Faculty of Life Sciences University of Manchester UK 3 Molecular Biology Division Department of Veterans Affairs MedicalCenter San Francisco CA USA 4 Department of Biochemistry Biophysics University of California San Francisco CA USA Keywords covalent flavinylation flavin post-translational redox potential self-catalytic Correspondence M. W. Fraaije Laboratory of Biochemistry Groningen Biomolecular Sciences and Biotechnology Institute University of Groningen Nijenborgh 4 9747 AG Groningen The Netherlands Fax 31 50 3634165 Tel 31 50 3634345 E-mail Received 12 February 2009 revised 26 March 2009 accepted 6 April 2009 Many enzymes use one or more cofactors such as biotin heme or flavin. These cofactors may be bound to the enzyme in a noncovalent or covalent manner. Although most flavoproteins contain a noncovalently bound flavin cofactor FMN or FAD a large number have these cofactors covalently linked to the polypeptide chain. Most covalent flavin-protein linkages involve a single cofactor attachment via a histidyl tyrosyl cysteinyl or threonyl linkage. However some flavoproteins contain a flavin that is tethered to two amino acids. In the last decade many studies have focused on elucidating the mechanism s of covalent flavin incorporation flavinyla-tion and the possible role s of covalent protein-flavin bonds. These endeavors have revealed that covalent flavinylation is a post-translational and self-catalytic process. This review presents an overview of the known types of covalent flavin bonds and the proposed mechanisms and roles of covalent flavinylation. doi .

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