Publication Date:
2009-05-22
Description:
Intramembrane proteolysis is increasingly seen as a regulatory step in a range of diverse processes, including development, organelle shaping, metabolism, pathogenicity and degenerative disease. Initial scepticism over the existence of intramembrane proteases was soon replaced by intense exploration of their catalytic mechanisms, substrate specificities, regulation and structures. Crystal structures of metal-dependent and serine intramembrane proteases have revealed active sites embedded in the plane of the membrane but accessible by water, a requirement for hydrolytic reactions. Efforts to understand how these membrane-bound proteases carry out their reactions have started to yield results.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erez, Elinor -- Fass, Deborah -- Bibi, Eitan -- England -- Nature. 2009 May 21;459(7245):371-8. doi: 10.1038/nature08146.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19458713" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Aspartic Acid Endopeptidases/metabolism
;
Cell Membrane/enzymology/*metabolism
;
Humans
;
Hydrolysis
;
Membrane Proteins/*metabolism
;
Metalloproteases/metabolism
;
Peptide Hydrolases/*metabolism
;
Serine Endopeptidases/metabolism
;
Substrate Specificity
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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