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Details on Person Rat HSL is inactivated by dephosphorylation. The catalyst of...
| Class:Id | Summation:163596 |
|---|---|
| _displayName | Rat HSL is inactivated by dephosphorylation. The catalyst of... |
| _timestamp | 2005-05-02 18:39:17 |
| created | [InstanceEdit:163566] D'Eustachio, P, 2005-05-02 18:38:43 |
| literatureReference | [LiteratureReference:163577] The protein phosphatases responsible for dephosphorylation of hormone-sensitive lipase in isolated rat adipocytes [LiteratureReference:163488] The regulatory and basal phosphorylation sites of hormone-sensitive lipase are dephosphorylated by protein phosphatase-1, 2A and 2C but not by protein phosphatase-2B [LiteratureReference:163491] Molecular mechanisms regulating hormone-sensitive lipase and lipolysis |
| text | Rat HSL is inactivated by dephosphorylation. The catalyst of this reaction is unknown. Protein phosphatases 1 and 2A are both abundant in rat adipocytes and both are active on HSL (Olsson and Belfrage 1987; Wood et al. 1993). Whether these enzymes act on phosphate groups attached to serine residues 659 and 660 of HSL is unknown, however (Holm et al. 2000). Although the reaction is annotated as though the phosphatase acts on phosphorylated HSL monomers, this also is unknown: does the HSL:FABP complex dissociate before HSL dephosphorylation (as implied here), or does dephosphorylation of HSL drive dissociation of the complex? Dephosphorylation of human HSL has not been studied in detail, so the human reaction is inferred from the well-studied rat one. |
| (summation) | [Reaction:163398] phosphorylated HSL + H2O -> HSL + orthophosphate [Rattus norvegicus] [Reaction:163489] phosphorylated HSL + H2O -> HSL + orthophosphate [Homo sapiens] |
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No pathways have been reviewed or authored by Rat HSL is inactivated by dephosphorylation. The catalyst of... (163596)
