Peptidaza Do
Peptidaza Do (EC 3.4.21.107, DegP, DegP proteaza, HtrA, proteaza A sa zahtevom za visoku temperaturu, HrtA protein toplotnog šoka, proteaza Do, Do proteaza) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Peptidaza Do | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| Peptidaza Do homo24mer, E.Coli | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.21.107 | ||||||||
| CAS broj | 161108-11-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- Ovaj enzim deluje na supstrate koji su bar delimično denaturisani. P1 ostatak mesta razlaganje je normalno između para hidrofobnih ostataka, kao što su Val-Val
Ova serinska endopeptidaza je esencijalna za razlaganje denaturisanih ili agregiranih proteina sa unutrašnje membrane i periplazmičnog prostora u Escherichia coli.
Reference uredi
- ↑ Lipinska, B., Zylicz, M. and Georgopoulos, C. (1990). „The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase”. J. Bacteriol. 172: 1791-1797. PMID 2180903.
- ↑ Seol, J.H., Woo, S.K., Jung, E.M., Yoo, S.J., Lee, C.S., Kim, K.J., Tanaka, K., Ichihara, A., Ha, D.B. and Chung, C.H. (1991). „Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product”. Biochem. Biophys. Res. Commun. 176: 730-736. PMID 2025286.
- ↑ Jones, C.H., Dexter, P., Evans, A.K., Liu, C., Hultgren, S.J. and Hruby, D.E. (2002). „Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin”. J. Bacteriol. 184: 5762-5771. PMID 12270835.
- ↑ Swamy, K.H., Chung, C.H. and Goldberg, A.L. (1983). „Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits”. Arch. Biochem. Biophys. 224: 543-554. PMID 6347072.
- ↑ Pallen, M.J. and Wren, B.W. (1997). „The HtrA family of serine proteases”. Mol. Microbiol. 26: 209-221. PMID 9383148.
- ↑ Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. and Clausen, T. (2002). „Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine”. Nature 416: 455-459. PMID 11919638.
Literatura uredi
- 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.