1. Endothelin converting enzyme-2: a processing enzyme involved in the generation of novel neuropeptides
- Author
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Nino Mzhavia, Lakshmi A. Devi, and Hui Pan
- Subjects
chemistry.chemical_classification ,Metalloproteinase ,Molecular Sequence Data ,Neuropeptides ,Metalloendopeptidases ,Peptide ,General Medicine ,Biology ,Endothelin-Converting Enzymes ,Subcellular localization ,Biochemistry ,Endothelin 1 ,Endothelin-Converting Enzyme 2 ,Protein Transport ,Enzyme ,chemistry ,Structural Biology ,Animals ,Aspartic Acid Endopeptidases ,Humans ,Amino Acid Sequence ,Peptide sequence ,Protein Processing, Post-Translational ,Intracellular - Abstract
Members of several metalloprotease families have been proposed to be involved in non-classical processing of neuroendocrine precursors. Among them, endothelin converting enzyme-2 (ECE-2) is a good candidate since it exhibits a neuroendocrine distribution, intracellular subcellular localization, and an acidic pH optimum. The enzyme is able to generate a number of biologically active peptides from peptide intermediates, suggesting an important role for this enzyme in the biosynthesis of regulatory peptides. These results are consistent with an important role for ECE-2 in the processing of regulatory peptides at non-classical sites.
- Published
- 2004