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Identification of essential aspartic acid and histidine residues of hormone-sensitive lipase : apparent residues of the catalytic triadOsterlund, Torben ; Contreras, Juan Antonio ; Holm, CeciliaIt is expected that hormone-sensitive lipase (HSL), like most other lipases and esterases, adopts an alpha/beta-hydrolase fold and has a catalytic triad of serine, aspartic or glutamic acid, and ... histidine. Recently, we have published a three-dimensional model for the C-terminal catalytic domain of HSL, having an alpha/beta-hydrolase fold and with Ser-423(1), Asp-703 and His-733 in the catalytic triad (Contreras et al. (1996) J. Biol. Chem. 271, 31426-31430). It has been shown that Ser-423, situated in the motif GXSXG, is essential for catalysis (Holm et al. (1994) FEBS Lett. 344, 234-238). The suggested aspartic acid and histidine were here probed by site-directed mutagenesis. Mutants of residues Asp-703 and His-733 are devoid of both lipaseand esterase activity, which is not the case for mutants of other testedaspartic acid and histidine residues. Thus, the presented data support the three-dimensional model structure with Asp-703 and His-733 as part of the traid.Source: FEBS letters. - ISSN 0014-5793 (Letn. 403, št. 3, 1997, str. 259-262)Type of material - article, component partPublish date - 1997Language - englishCOBISS.SI-ID - 21679065
Author
Osterlund, Torben |
Contreras, Juan Antonio |
Holm, Cecilia
Topics
Animals |
Aspartic Acid |
Physiology |
Binding Sites |
Cos Cells |
Catalysis |
Cholesterol Esterase |
Genetics |
Metabolism |
Histidine |
Physiology |
Models, Molecular |
Mutagenesis, Site-Directed |
Rats |
Aspartna kislina |
COS celice |
Histidin |
Holesterolna esteraza |
Kataliza |
Mesta vezave |
Modeli molekularni |
Mutageneza, mesto-usmerjena |
Podgane |
Živali
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Osterlund, Torben | ![]() |
Contreras, Juan Antonio | 28452 |
Holm, Cecilia | ![]() |
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