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
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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

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  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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