title: The Serine Recombinases.
abstract: In site-specific recombination, two short DNA sequences ('sites') are each cut at specific points in both strands, and the cut ends are rejoined to new partners. The enzymes that mediate recognition of the sites and the subsequent cutting and rejoining steps are called recombinases. Most recombinases fall into one of two families according to similarities of their protein sequences and mechanisms; these families are known as the tyrosine recombinases and the serine recombinases, the names referring to the conserved amino acid residue that attacks the DNA phosphodiester and becomes covalently linked to a DNA strand end during catalysis. This chapter gives an overview of our current understanding of the serine recombinases, their types, biological roles, structures, catalytic mechanisms, mechanisms of regulation, and applications.
authors.affiliation: Institute of Molecular, Cell and Systems Biology, University of Glasgow, Bower Building, Glasgow G12 8QQ, Scotland, United Kingdom.
authors.forename: W Marshall
authors.initials: WM
authors.lastname: Stark
mesh_terms: D004247:DNA / Q000235:genetics* / Q000378:metabolism*; D045522:Recombinases / Q000737:chemistry / Q000145:classification* / Q000235:genetics / Q000378:metabolism*; D011995:Recombination, Genetic; D012694:Serine / Q000378:metabolism*
chemical_list: D045522:Recombinases; D012694:Serine; D004247:DNA