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Evidence for a multi‐domain structure for hormone‐sensitive lipase
Author(s) -
Smith Gabriele M.,
Garton Andrew J.,
Aitken Alastair,
Yeaman Stephen J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01076-9
Subject(s) - hormone sensitive lipase , lipase , biochemistry , chemistry , phosphorylation , enzyme
Hormone‐sensitive lipase (HSL) is a multi‐functional enzyme involved in several aspects of lipid metabolism. Limited tryptic digestion of HSL led to selective loss of activity against lipid substrates but not against the water‐soluble substrate, p ‐nitrophenyl butyrate. Following labelling of the active site of HSL with either [ 3 H]di‐isopropylfluorophosphate or [ 14 C]orlistat, tryptic digestion of HSL generated a stable radiolabelled domain of molecular mass approx. 17.6 kDa, consistent with this representing a catalytic domain of HSL capable of hydrolysing water‐soluble but not lipid substrates. Following phosphorylation of HSL by cyclic AMP‐dependent protein kinase, limited tryptic digestion produced a stable phosphorylated domain of molecular mass 11.5 kDa. Based on these experimental data a model for a domain structure of HSL is proposed.