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Protein Engineering, Vol. 13, No. 10, 711-717, October 2000
© 2000 Oxford University Press

Analysis of the psychrotolerant property of hormone-sensitive lipase through site-directed mutagenesis

Henrik Laurell1,2, Juan Antonio Contreras1, Isabelle Castan3, Dominique Langin3 and Cecilia Holm1,4

1 Section for Molecular Signalling, Department of Cell and Molecular Biology, Lund University, PO Box 94, S-221 00 Lund, Sweden and 3 Unité INSERM 317, Institut Louis Bugnard, Hôpital Rangueil, F-31403 Toulouse Cedex 4, France

Mammalian hormone-sensitive lipase (HSL) has given its name to a family of primarily prokaryotic proteins which are structurally related to type B carboxylesterases. In many of these {alpha}/ß hydrolases, a conserved HG-dipeptide flanks the catalytic pocket. In HSL this dipeptide is followed by two additional glycine residues. Through site-directed mutagenesis, we have investigated the importance of this motif for enzyme activity. Since the presence of multiple glycine residues in a critical region could contribute to cold adaptation by providing local flexibility, we studied the effect of mutating these residues on the psychrotolerant property of HSL. Any double mutation rendered the enzyme completely inactive, without any major effect on the enzyme stability. The partially active single mutants retained the same proportion of activity at reduced temperatures as the wild-type enzyme. These results do not support a role for the HGGG motif in catalysis at low temperatures, but provide further validation of the current three-dimensional model of HSL. Rat HSL was found to be relatively more active than human HSL at low temperatures. This difference was, however, not due to the 12 amino acids which are present in the regulatory module of the rat enzyme but absent in human HSL.


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