Signal peptidase II (EC 3.4.23.36, premurein-leader peptidase, prolipoprotein signal peptidase, leader peptidase II, premurein leader proteinase) is an enzyme.[1][2][3]
Signal peptidase II | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.23.36 | ||||||||
CAS no. | 171715-14-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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This enzyme catalyses a chemical reaction. It releases signal peptides from murein prolipoprotein and other bacterial membrane prolipoproteins. It also hydrolyses -Xaa-Yaa-Zaa-(S,diacylglyceryl)Cys-, in which Yaa (Ala or Ser) and Zaa (Gly or Ala) have small neutral sidechains, and Xaa is hydrophobic (preferably Leu).
This enzyme is present in bacterial inner membranes.
References
edit- ^ Dev IK, Ray PH (June 1990). "Signal peptidases and signal peptide hydrolases". Journal of Bioenergetics and Biomembranes. 22 (3): 271–90. doi:10.1007/bf00763168. PMID 2202720.
- ^ Zhao XJ, Wu HC (March 1992). "Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene". FEBS Letters. 299 (1): 80–4. doi:10.1016/0014-5793(92)80105-p. PMID 1544479.
- ^ Sankaran K, Wu HC (1995). Bacterial prolipoprotein signal peptidase. Methods in Enzymology. Vol. 248. pp. 169–80. doi:10.1016/0076-6879(95)48014-5. PMID 7674920.
External links
edit- Signal+peptidase+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH)