Tripeptidilna peptidaza I

Izvor: Wikipedia
Tripeptidilna peptidaza I
3EE6.png
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 structures

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

Odvajanje N-terminalnog tripeptida sa polipeptida. Takođe deluje kao endopeptidaza.

Ovaj lizozomalni enzim je aktivan pri kiselom pH.

Reference[uredi - уреди]

  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 - уреди]

Spoljašnje veze[uredi - уреди]