Seralizin
| Seralizin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.24.40 | ||||||||
| CAS broj | 70851-98-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Seralizin (EC 3.4.24.40, Pseudomonas aeruginosa alkalinska proteinaza, Escherichia freundii proteinaza, Serratia marcescens ekstraćelijska proteinaza, Serratia marcescens metaloproteinaza, Pseudomonas aeruginosa alk. proteaza, Serratia marcescens metaloproteaza) je enzim.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Preferentno razlaganje veza sa hidrofobnim ostacima u P1'
Ova endopeptidaza je prisutna u Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens i Erwinia chrysanthemi.
- ↑ Morihara, K., Tsuzuki, H. and Oka, T. (1968). „Comparison of the specificities of various neutral proteinases from microorganisms”. Arch. Biochem. Biophys. 123: 572-588. PMID 4967801.
- ↑ Morihara, K., Tsuzuki, H. and Oka, T. (1973). „On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides”. Biochim. Biophys. Acta 309: 414-429. PMID 4199986.
- ↑ Nakajima, M., Mizusawa, K. and Yoshida, F. (1974). „Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii”. Eur. J. Biochem. 44: 87-96. PMID 4212288.
- ↑ Decedue, C.J., Broussard, E.A., II, L arson, A.D. and Braymer, H.D. (1979). „Purification and characterization of the extracellular proteinase of Serratia marcescens”. Biochim. Biophys. Acta 569: 293-301. PMID 383155.
- ↑ Doerr, M. and Traub, W.H. (1984). „Purification and characterization of two Serratia marcescens proteases”. Zentralbl. Bakteriol., Mikrobiol. Hyg. Ser. A 257: 6-19. PMID 6380155.
- ↑ Nakahama, K., Yoshimura, K., Marumoto, R., Kikuchi, M., Lee, I.S., Hase, T. and Matsubara, H. (1986). „Cloning and sequencing of Serratia protease gene”. Nucleic Acids Res. 14: 5843-5856. PMID 3016665.
- ↑ Dahler, G.S., Barras, F. and Keen, N.T. (1990). „Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16”. J. Bacteriol. 172: 5803-5815. PMID 2211513.
- ↑ Okuda, K., Morihara, K., Atsumi, Y., Takeuchi, H., Kawamoto, S., Kawasaki, H., Suzuki, K. and Fukushima, J. (1990). „Complete nucleotide sequence of the structural gene for alkaline proteinase from Pseudomonas aeruginosa IFO 3455”. Infect. Immun. 58: 4083-4088. PMID 2123832.
- 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.