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Domain-structure analysis of recombinant rat hormone-sensitive lipaseOsterlund, Torben ...Hormone-sensitive lipase (HSL) plays a key role in lipid metabolism and overall energy homoeostasis, by controlling the release of fatty acids from stored triglycerides in adipose tissue. Lipases and ... esterases form a protein superfamily with a common structural fold, called the alpha/beta-hydrolase fold, and a catalytic triad of serine, aspartic or glutamic acid and histidine. Previous alignments between HSL and lipase 2 of Moraxella TA144 have been extended to cover a much larger part of the HSL sequence. From theseextended alignments, possible sites for the catalytic triad and alpha/beta-hydrolase fold are suggested. Furthermore, it is proposed that HSL contains a structural domain with catalytic capacity and a regulatory module attached, as well as a structural N-terminal domain unique to this enzyme. In order to test the proposed domain structure, rat HSL was overexpressed and purified to homogeneity using a baculovirus/insect-cell expression system. Thepurification, resulting in > 99% purity, involved detergent solubilization followed by anion-exchange chromatography and hydrophobic-interaction chromatography. The purified recombinant enzyme was identical to rat adipose-tissue HSL with regard to specific activity, substrate specificity andability to serve as a substrate for cAMP-dependent protein kinase. The recombinant HSL was subjected to denaturation by guanidine hydrochloride and limited proteolysis. These treatments resulted in more extensive loss of activity against phospholipid-stabilized lipid substrates than against water-soluble substrates, suggesting that the hydrolytic activity can be separated from recognition of lipid substrates. These data support the conceptthat HSL has at least two major domains.Source: Biochemical journal. - ISSN 0264-6021 (Letn. 319, 1996, str. 411-420)Type of material - article, component partPublish date - 1996Language - englishCOBISS.SI-ID - 21678297
Author
Osterlund, Torben |
Danielsson, Birgitta |
Degerman, Eva |
Contreras, Juan Antonio |
Edgren, Gudrun |
Davis, Richard C. |
Schotz, Michael C. |
Holm, Cecilia
Topics
Amino Acid Sequence |
Animals |
Cholesterol Esterase |
Chemistry |
Genetics |
Metabolism |
Molecular Sequence Data |
Rats |
Recombinant Proteins |
Chemistry |
Genetics |
Metabolism |
Sequence Alignment |
Sequence Analysis |
Aminokislinsko zaporedje |
Holesterolna esteraza |
Molekulsko zaporedje, podatki |
Podgane |
Rekombinantne beljakovine |
Zaporedje razvrstitev |
Zaporedje, analiza |
Živali
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Osterlund, Torben | ![]() |
Danielsson, Birgitta | ![]() |
Degerman, Eva | ![]() |
Contreras, Juan Antonio | 28452 |
Edgren, Gudrun | ![]() |
Davis, Richard C. | ![]() |
Schotz, Michael C. | ![]() |
Holm, Cecilia | ![]() |
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