title: News from the interface: the molecular structures of triacylglyceride lipases.
abstract: Neutral lipases constitute one of the most ubiquitous and diverse families of enzymes. The recently solved crystal structures of three lipases show that enzymatic hydrolysis occurs with the assistance of a catalytic triad, which is structurally reminiscent of serine proteinases. However, these lipases only become active at the oil-water interface through a conformational change that exposes the active centre of the enzyme.
authors.affiliation: Department of Biochemistry, University of Alberta, Edmonton, Canada.
authors.forename: Z S
authors.initials: ZS
authors.lastname: Derewenda
authors.forename: A M
authors.initials: AM
authors.lastname: Sharp
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008049:Lipase / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D013329:Structure-Activity Relationship
chemical_list: D008049:Lipase