Tripeptidilna peptidaza I

Tripeptidilna peptidaza I (EC 3.4.14.9, tripeptidilna aminopeptidaza, tripeptidilna peptidaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Tripeptidilna peptidaza I
Identifikatori
EC broj 3.4.14.9
CAS broj 151662-36-1
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Odvajanje N-terminalnog tripeptida sa polipeptida. Takođe deluje kao endopeptidaza.

Ovaj lizozomalni enzim je aktivan pri kiselom pH.

Reference uredi

  1. Ezaki, J., Tanida, I., Kanehagi, N. and Kominami, E. (1999). „A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase”. J. Neurochem. 72: 2573-2582. PMID 10349869. 
  2. Rawlings, N.D. and Barrett, A.J. (1999). „Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis”. Biochim. Biophys. Acta 1429: 496-500. PMID 9989235. 
  3. Ezaki, J., Takeda-Ezaki, M., Oda, K. and Kominami, E. (2000). „Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis”. Biochem. Biophys. Res. Commun. 268: 904-908. PMID 10679303. 
  4. Junaid, M.A., Wu, G.X. and Pullarkat, R.K. (2000). „Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis”. J. Neurochem. 74: 287-294. PMID 10617131. 
  5. Lin, L., Sohar, I., Lackland, H. and Lobel, P. (2001). „The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH”. J. Biol. Chem. 276: 2249-2255. PMID 11054422. 

Literatura uredi

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