Biology:Signal peptidase I
From HandWiki
| Signal peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.89 | ||||||||
| CAS number | 65979-36-4 | ||||||||
| 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 I (EC 3.4.21.89, 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, signalase, bacterial leader peptidase 1) is an enzyme.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- Cleavage of hydrophobic, N-terminal signal or leader sequences
This enzyme is present in bacterial membranes and in chloroplast thylakoid membranes.
References
- ↑ "Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad". Journal of Bacteriology 175 (16): 4957–61. August 1993. doi:10.1128/jb.175.16.4957-4961.1993. PMID 8394311.
- ↑ "A mitochondrial protease with two catalytic subunits of nonoverlapping specificities". Science 262 (5142): 1997–2004. December 1993. doi:10.1126/science.8266095. PMID 8266095.
- ↑ "A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase". The Journal of Biological Chemistry 268 (36): 27349–54. December 1993. PMID 8262975.
- ↑ Eukaryote microsomal signal peptidases. Methods in Enzymology. 244. 1994. pp. 301–14. doi:10.1016/0076-6879(94)44024-7.
- ↑ Bacterial leader peptidase 1. Methods in Enzymology. 244. 1994. pp. 285–301. doi:10.1016/0076-6879(94)44023-9.
- ↑ "Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana. Implications for the origin and catalytic mechanism of the enzyme". The Journal of Biological Chemistry 273 (2): 689–92. January 1998. doi:10.1074/jbc.273.2.689. PMID 9422718.
- ↑ "Complete maturation of the plastid protein translocation channel requires a type I signal peptidase". The Journal of Cell Biology 171 (3): 425–30. November 2005. doi:10.1083/jcb.200506171. PMID 16275749. PMC 2171254. http://orca.cf.ac.uk/64414/1/200506171.pdf.
External links
- Signal+peptidase+I at the US National Library of Medicine Medical Subject Headings (MeSH)
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