Signal peptidase II

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
Identifiers
EC no.3.4.23.36
CAS no.171715-14-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

  1. 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.
  2. 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.
  3. 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.
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