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
In molecular biology, the Signal Peptide Peptidase (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmemb ...
'', ''signalase'', ''bacterial leader peptidase 1'') is an
enzyme.
This enzyme
catalyses the following
chemical reaction
: Cleavage of
hydrophobic,
N-terminal
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the ami ...
signal or leader sequences
This enzyme is present in bacterial membranes and in
chloroplast
A chloroplast () is a type of membrane-bound organelle known as a plastid that conducts photosynthesis mostly in plant and algal cells. The photosynthetic pigment chlorophyll captures the energy from sunlight, converts it, and stores it in ...
thylakoid membranes.
References
External links
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EC 3.4.21