Meprin-A
| Meprin-A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.24.18 | ||||||||
| CAS broj | 148938-24-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Meprin-A (EC 3.4.24.18, endopeptidaza-2, meprin, hidrolaza N-benzoil-L-tirozil-p-aminobenzojeve kiseline, PABA-peptidna hidrolaza, PPH) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Hidroliza proteinskih i peptidnih supstrata preferentno na karboksilnoj strani hidrofobnih ostataka
Ova membranska metaloendopeptidaza je prisutna u bubrezima pacova i miševa.
Reference
- ↑ Beynon, R.J., Shannon, J.D. and Bond, J.S. (1981). „Purification and characterization of a metallo-endoproteinase from mouse kidney”. Biochem. J. 199: 591-598. PMID 7041888.
- ↑ Butler, P.E., McKay, M.J. and Bond, J.S. (1987). „Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney”. Biochem. J. 241: 229-235. PMID 3105525.
- ↑ Stephenson, S.L. and Kenny, A.J. (1988). „The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme 'endopeptidase-2′ and by rat microvillar membranes”. Biochem. J. 255: 45-51. PMID 2461706.
- ↑ Sterchi, E.E., Naim, H.Y., Lentze, M.J., Hauri, H.-P. Fransen, J.A.M. (1988). „N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides”. Arch. Biochem. Biophys. 265: 105-118. PMID 3261961.
- ↑ Barnes, K., Ingram, J. and Kenny, A.J. (1989). „Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse”. Biochem. J. 264: 335-346. PMID 2690825.
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 Meprin+A
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
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
