Leader Peptidase
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Leader Peptidase
Signal peptidase I (, ''leader peptidase I'', ''signal proteinase'', ''Escherichia coli leader peptidase'', ''eukaryotic signal peptidase'', ''eukaryotic signal proteinase'', ''leader peptidase'', ''leader peptide hydrolase'', ''leader proteinase'', ''signal peptidase'', ''pilin leader peptidase'', ''SPC'', ''prokaryotic signal peptidase'', ''prokaryotic leader peptidase'', ''HOSP'', ''prokaryotic signal proteinase'', ''propeptidase'', ''PuIO prepilin peptidase'', ''signal peptide hydrolase'', ''signal peptide peptidase'', ''signalase'', ''bacterial leader peptidase 1'') is an enzyme. This enzyme catalyses the following chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ... : Cleavage of hydrophobic, N-terminal signal or leader sequences This enzyme is present in bact ...
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Signal Peptidase
Signal peptidases are enzymes that convert secretory and some membrane proteins to their mature or pro forms by cleaving their signal peptides from their N-termini. Signal peptidases were initially observed in endoplasmic reticulum (ER)-derived membrane fractions isolated from mouse myeloma cells. The key observation by César Milstein and colleagues was that immunoglobulin light chains were produced in a higher molecular weight form, which became processed by the ER membrane fraction. This finding was directly followed by the discovery of the translocation machinery. Signal peptidases are also found in prokaryotes as well as the protein import machinery of mitochondria and chloroplasts. All signal peptidases described so far are serine proteases. The active site that endoproteolytically cleaves signal peptides from translocated precursor proteins is located at the extracytoplasmic site of the membrane. The eukaryotic signal peptidase is an integral membrane protein Me ...
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