Signal peptidase I

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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. 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

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.

External links

Signal+peptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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EC 3.4.21