| Signal peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.89 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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.
- ^ Black MT (August 1993). "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. doi: 10.1128/jb.175.16.4957-4961.1993. PMC 204959. PMID 8394311.
- ^ Nunnari J, Fox TD, Walter P (December 1993). "A mitochondrial protease with two catalytic subunits of nonoverlapping specificities". Science. 262 (5142): 1997–2004. doi: 10.1126/science.8266095. PMID 8266095.
- ^ Tschantz WR, Sung M, Delgado-Partin VM, Dalbey RE (December 1993). "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. PMID 8262975.
- ^ Lively MO, Newsome AL, Nusier M (1994). Eukaryote microsomal signal peptidases. Methods in Enzymology. Vol. 244. pp. 301–14. doi: 10.1016/0076-6879(94)44024-7. PMID 7845216.
- ^ Tschantz WR, Dalbey RE (1994). Bacterial leader peptidase 1. Methods in Enzymology. Vol. 244. pp. 285–301. doi: 10.1016/0076-6879(94)44023-9. PMID 7845215.
- ^ Chaal BK, Mould RM, Barbrook AC, Gray JC, Howe CJ (January 1998). "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. doi: 10.1074/jbc.273.2.689. PMID 9422718.
- ^ Inoue K, Baldwin AJ, Shipman RL, Matsui K, Theg SM, Ohme-Takagi M (November 2005). "Complete maturation of the plastid protein translocation channel requires a type I signal peptidase" (PDF). The Journal of Cell Biology. 171 (3): 425–30. doi: 10.1083/jcb.200506171. PMC 2171254. PMID 16275749.
- Signal+peptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Signal peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.89 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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.
- ^ Black MT (August 1993). "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. doi: 10.1128/jb.175.16.4957-4961.1993. PMC 204959. PMID 8394311.
- ^ Nunnari J, Fox TD, Walter P (December 1993). "A mitochondrial protease with two catalytic subunits of nonoverlapping specificities". Science. 262 (5142): 1997–2004. doi: 10.1126/science.8266095. PMID 8266095.
- ^ Tschantz WR, Sung M, Delgado-Partin VM, Dalbey RE (December 1993). "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. PMID 8262975.
- ^ Lively MO, Newsome AL, Nusier M (1994). Eukaryote microsomal signal peptidases. Methods in Enzymology. Vol. 244. pp. 301–14. doi: 10.1016/0076-6879(94)44024-7. PMID 7845216.
- ^ Tschantz WR, Dalbey RE (1994). Bacterial leader peptidase 1. Methods in Enzymology. Vol. 244. pp. 285–301. doi: 10.1016/0076-6879(94)44023-9. PMID 7845215.
- ^ Chaal BK, Mould RM, Barbrook AC, Gray JC, Howe CJ (January 1998). "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. doi: 10.1074/jbc.273.2.689. PMID 9422718.
- ^ Inoue K, Baldwin AJ, Shipman RL, Matsui K, Theg SM, Ohme-Takagi M (November 2005). "Complete maturation of the plastid protein translocation channel requires a type I signal peptidase" (PDF). The Journal of Cell Biology. 171 (3): 425–30. doi: 10.1083/jcb.200506171. PMC 2171254. PMID 16275749.
- Signal+peptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)