Glutamatna karboksipeptidaza II
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
| Glutamatna karboksipeptidaza II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| 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 | ||||||||
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- 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.
ReferenceUredi
- ↑ 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.
- ↑ Rawlings, N.D. and Barrett, A.J. (1997). „Structure of membrane glutamate carboxypeptidase”. Biochim. Biophys. Acta 1339: 247-252. PMID 9187245.
- ↑ 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.
- ↑ 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.
LiteraturaUredi
- 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.