Glutamatna karboksipeptidaza II

Glutamatna karboksipeptidaza II
Identifikatori
EC broj 3.4.17.21
CAS broj 9074-87-7
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search

Glutamatna karboksipeptidaza II (EC 3.4.17.21, N-acetilisana-gama-vezana-kiselinska dipeptidaza (NAALADaza), folatna hidrolaza, prostat-specifični membranski antigen, pteroilpoli-gama-glutamatna karboksipeptidaza, mikrozomalna gama-glutamilna karboksipeptidaza, pteroilpoliglutamatna hidrolaza, folilpoliglutamatna hidrolaza, pteroilpoli-gama-glutamatna hidrolaza, pteroilpoligamaglutamilna hidrolaza, pteroilpoliglutamatna hidrolaza, pteroilpoliglutaminsko kiselinska hidrolaza, PSM antigen, acetilaspartilglutamatna dipeptidaza, NAALA dipeptidaza, NAAG peptidaza pacova, mGCP, membranska glutamatna karboksipeptidaza, N-acetilisana-alfa-vezana-amino dipeptidaza, prostratno-specifični membranski antigen, N-acetilisana alfa-vezana kiselinska dipeptidaza, PSMA) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Odvajanje nesupstituisanog, C-terminalnog glutaminskog ostatka, tipično sa Ac-Asp-Glu ili folilpoli-gama-glutamata

Ova metalo-karboksipeptidaza je predominantno izražena kao membranski enzim koji je težak 94-100 kDa.

Reference

  1. Heston, W.D.W. (1997). „Characterization and glutamyl preferring carboxypeptidase function of prostate specific membrane antigen: a novel folate hydrolase”. Urology 49: 104-112. PMID 9123729. 
  2. Rawlings, N.D. and Barrett, A.J. (1997). „Structure of membrane glutamate carboxypeptidase”. Biochim. Biophys. Acta 1339: 247-252. PMID 9187245. 
  3. Halsted, C.H., Ling, E.-H., Luthi-Carter, R., Villanueva, J.A., Gardner, J.M., Coyle, J.T. (1998). „Folylpoly-γ-glutamate carboxypeptidase from pig jejunum: molecular characterization and relation to glutamate carboxypeptidase II”. J. Biol. Chem. 273: 20417-20424. PMID 9685395. 
  4. Luthi-Carter, R., Berger, U.V., Barczak, A.K., Enna, M. and Coyle, J.T. (1998). „Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II”. Proc. Natl. Acad. Sci. USA 95: 3215-3220. PMID 9501243. 

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

  • MeSH Glutamate+carboxypeptidase+II
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TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6