Keksin
| Keksin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.21.61 | ||||||||
| CAS broj | 99676-46-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Keksin (EC 3.4.21.61, proteinaza yscF, prohormon-transformišuća endoproteaza, uparena-bazna endopeptidaza, kvaščana cisteinska proteinaza F, uparena-bazna endopeptidaza, andrenorfin-Gly-generišući enzim, endoproteinaza Kex2p, gen KEX2 dibazna proteinaza, Kex 2p proteinaza, Kex2 endopeptidaza, Kex2 endoproteaza, Kex2 endoproteinaza, Kex2 proteaza, proteinaza Kex2p, proteinaza transformacije prohormona, proproteinska konvertaza, proteaza KEX2, Kex2 proteinaza, Kex2-slična endoproteinaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Razlaganje -Lys-Arg- i -Arg-Arg- veza u kvaščanom alfa-faktorskom feromonu i prekursorima smrtonisnih toksina
Ova peptidaza se aktivira jonom Ca2+.
Reference
- ↑ Julius, D., Brake, A., Blair, L., Kunisawa, R. and Thorner, J. (1984). „Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor”. Cell 37: 1075-1089. PMID 6430565.
- ↑ Achstetter, T. and Wolf, D.H. (1985). „Hormone processing and membrane-bound proteinases in yeast”. EMBO J. 4: 173-177. PMID 3894003.
- ↑ Mizuno, K., Nakamura, T., Ohshima, T., Tanaka, S. and Matsuo, H. (1988). „Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases”. Biochem. Biophys. Res. Commun. 156: 246-254. PMID 2845974.
- ↑ Fuller, R.S., Brake, A. and Thorner, J. (1989). „Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease”. Proc. Natl. Acad. Sci. USA 86: 1434-1438. PMID 2646633.
- ↑ Mizuno, K., Nakamura, T., Ohshima, T., Tanaka, S. and Matsuo, H. (1989). „Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae”. Biochem. Biophys. Res. Commun. 159: 305-311. PMID 2845974.
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 Kexin
- 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
