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Sökning: onr:"swepub:oai:lup.lub.lu.se:3bb7f944-ec9c-440f-b8dd-c3658b1abb7d" > Domain-structure an...

  • Österlund, TorbenLund University,Lunds universitet,Institutionen för translationell medicin,Medicinska fakulteten,Department of Translational Medicine,Faculty of Medicine (författare)

Domain-structure analysis of recombinant rat hormone-sensitive lipase

  • Artikel/kapitelEngelska1996

Förlag, utgivningsår, omfång ...

  • 1996

Nummerbeteckningar

  • LIBRIS-ID:oai:lup.lub.lu.se:3bb7f944-ec9c-440f-b8dd-c3658b1abb7d
  • https://lup.lub.lu.se/record/1109898URI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:art swepub-publicationtype
  • Ämneskategori:ref swepub-contenttype

Anmärkningar

  • 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 these extended 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. The purification, 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 and ability 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 concept that HSL has at least two major domains.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Danielsson, BirgittaLund University,Lunds universitet,Molekylär endokrinologi,Forskargrupper vid Lunds universitet,Molecular Endocrinology,Lund University Research Groups(Swepub:lu)medk-bda (författare)
  • Degerman, EvaLund University,Lunds universitet,Signaltransduktionsforskning,Forskargrupper vid Lunds universitet,Insulin Signal Transduction,Lund University Research Groups(Swepub:lu)medk-ede (författare)
  • Contreras, Juan AntonioLund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Department of Experimental Medical Science,Faculty of Medicine(Swepub:lu)medk-jac (författare)
  • Edgren, Gudrun (författare)
  • Davis, Richard C (författare)
  • Schotz, Michael C (författare)
  • Holm, CeciliaLund University,Lunds universitet,Molekylär endokrinologi,Forskargrupper vid Lunds universitet,Molecular Endocrinology,Lund University Research Groups(Swepub:lu)medk-cho (författare)
  • Institutionen för translationell medicinMedicinska fakulteten (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Biochemical Journal319:Pt 2, s. 411-4200264-6021

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