Structure-function relationships of hormone-sensitive lipase

Research into the structure-function relationships of lipases and esterases has increased significantly during the past decade. Of particular importan ce has been the deduction of several crystal structures, providing a new ba sis for understanding these enzymes. The generated insights have, together with cloning and expression, aided studies on structure-function relationsh ips of hormone-sensitive lipase (HSL). Novel phosphorylation sites have bee n identified in HSL, which are probably important for activation of HSL and lipolysis. Functional and structural analyses have revealed features in HS L common to lipases and esterases. In particular, the catalytic core with a catalytic triad has been unveiled. Furthermore, the investigations have gi ven clear suggestions with regard to the identity of functional and structu ral domains of HSL. In the present paper, these studies on HSL structure-fu nction relationships and short-term regulation are reviewed, and the result s presented in relation to other discoveries in regulated lipolysis.