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  • Identification of essential aspartic acid and histidine residues of hormone-sensitive lipase : apparent residues of the catalytic triad
    Osterlund, Torben ; Contreras, Juan Antonio ; Holm, Cecilia
    It 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.
    Vir: FEBS letters. - ISSN 0014-5793 (Letn. 403, št. 3, 1997, str. 259-262)
    Vrsta gradiva - članek, sestavni del
    Leto - 1997
    Jezik - angleški
    COBISS.SI-ID - 21679065

vir: FEBS letters. - ISSN 0014-5793 (Letn. 403, št. 3, 1997, str. 259-262)
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