Biology:Signal peptidase II
From HandWiki
| Signal peptidase II | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.23.36 | ||||||||
| CAS number | 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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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]
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
- ↑ "Signal peptidases and signal peptide hydrolases". Journal of Bioenergetics and Biomembranes 22 (3): 271–90. June 1990. doi:10.1007/bf00763168. PMID 2202720.
- ↑ "Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene". FEBS Letters 299 (1): 80–4. March 1992. doi:10.1016/0014-5793(92)80105-p. PMID 1544479. Bibcode: 1992FEBSL.299...80Z.
- ↑ "Bacterial prolipoprotein signal peptidase". Proteolytic Enzymes: Aspartic and Metallo Peptidases. Methods in Enzymology. 248. 1995. pp. 169–80. doi:10.1016/0076-6879(95)48014-5. ISBN 978-0-12-182149-4.
External links
- Signal+peptidase+II at the US National Library of Medicine Medical Subject Headings (MeSH)
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