Termolizin
| Termolizin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.24.27 | ||||||||
| CAS broj | 9073-78-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Termolizin (EC 3.4.24.27, Bacillus thermoproteolyticus neutralna proteinaza, termoaza, termoaza Y10, TLN) je enzim.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Preferentno razlaganje: -Leu > -Phe
Ova termostabilna ekstracelularna metaloendopeptidaza sadrži četiri jona kalcijuma.
Reference
- ↑ Ohta, Y. Ogura, Y. and Wada, A. (1966). „Thermostable protease from thermophilic bacteria. I. Thermostability, physicochemical properties, and amino acid composition”. J. Biol. Chem. 241: 5919-5925. PMID 5954368.
- ↑ 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.
- ↑ Latt, S. (1969). „A., Holmquist, B. and Vallee, B. L. Thermolysin: a zinc metalloenzyme”. Biochem. Biophys. Res. Commun. 37: 333-339. PMID 5823940.
- ↑ Desmazeaud, M. (1971). „J. and Hermier, J. H. Spécificité de la protéase neutre de Micrococcus caseolyticus”. Eur. J. Biochem. 19: 51-55. PMID 5551628.
- ↑ Morihara, K. and Tsuzuki, H. (1971). „Comparative study of various neutral proteinases from microorganisms: specificity with oligopeptides”. Arch. Biochem. Biophys. 146: 291-296. PMID 5004124.
- ↑ Titani, K., Hermodson, M. (1972). „A., Ericson, L. H., Walsh, K. A. and Neurath, H. Amino-acid sequence of thermolysin”. Nature New Biol. 238: 35-37.
- ↑ Matthews, B. (1988). „W. Structural basis of the action of thermolysin and related zinc peptidases”. Acc. Chem. Res. 21: 333-340.
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 Thermolysin
- 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
