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Karboksipeptidaza E

Izvor: Wikipedija
Karboksipeptidaza E
Identifikatori
EC broj 3.4.17.10
CAS broj 81876-95-1
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Karboksipeptidaza E (EC 3.4.17.10, karboksipeptidaza H, enkefalinska konvertaza, kobaltom stimulisana hromafin granularna karboksipeptidaza, enkefalinska konvertaza, membranska karboksipeptidaza, enkefalinska prekursorska endopeptidaza, enkefalinska prekursorska karboksipeptidaza, peptidilna-L-lizin(-L-arginin) hidrolaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Odvajanje C-terminalnog arginina ili lizina sa polipeptida

Ovaj cinkov enzim aktivira jon Co2+.

Reference

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  1. Qian, Y.M., Varlamov, O. and Fricker, L.D. (1999). „Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway”. J. Biol. Chem. 274: 11582-11586. PMID 10206965. 
  2. Fricker, L.D. (1998). „Carboxypeptidase E/H”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes. London: Academic Press. str. 1341-1344. 
  3. Fricker, L.D. (1995). „Methods for studying carboxypeptidase E”. Methods Neurosci. 23: 237-250. 
  4. Manser, E., Fernandez, D. (1990). „, Loo,L., Goh, P.Y., Monfries, C., Hall, C. and Lim, L. Human carboxypeptidase E: isolation and characterisaton of the cDNA, sequence conservation, expression and processing in vitro”. Biochem. J. 267: 517-525. PMID 2334405. 
  5. Fricker, L.D. (1988). „Carboxypeptidase E”. Annu. Rev. Physiol. 50: 309-321. PMID 2897826. 

Literatura

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  • Fricker, L.D. (1998). „Carboxypeptidase E/H”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes. London: Academic Press. str. 1341-1344. 

Vanjske veze

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