News from the interface: the molecular structures of triacylglyceride lipases.
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.
Derewenda
Z S
ZS
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Sharp
A M
AM
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
D008049:Lipase