Beta-laktamaza
Beta-laktamaza | |||||||||
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Metallo-beta-laktamaza L1 homotetramer, Stenotrophomonas maltophilia | |||||||||
Identifikatori | |||||||||
EC broj | 3.5.2.6 | ||||||||
CAS broj | 9073-60-3 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Beta-laktamaza (EC 3.5.2.6, penicilinaza, cefalosporinaza, neutrapen, penicilinska beta-laktamaza, eksopenicilinaza, ampicillinaza, penicilin amido-beta-laktamhidrolaza, penicilinaza I, II, beta-laktamaza I-III, beta-laktamaza A, B, C, beta-laktamaza AME I, cefalosporin-beta-laktamaza) je enzim sa sistematskim imenom beta-laktam hidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- beta-laktam + H2O supstituisana beta-aminokiselina
Ova grupa enzima ima promenljivu specifičnost hidrolize beta-laktama.
Reference
- ↑ Citri, N. (1971). „Penicillinase and other β-lactamases”. u: Boyer, P.D.. The Enzymes. 4 (3rd izd.). New York: Academic Press. str. 23-46.
- ↑ Hennessey, T.D. and Richmond, M.H. (1968). „The purification and some properties of a β-lactamase (cephalosporinase) synthesized by Enterobacter cloacae”. Biochem. J. 109: 469-473. PMID 5685878.
- ↑ Kuwabara, S. (1970). „Purification and properties of two extracellular β-lactamases from Bacillus cereus 569-H”. Biochem. J. 118: 457-465. PMID 4990588.
- ↑ Pollock, M.R. (1960). „Penicillinase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 4 (2nd izd.). New York: Academic Press. str. 269-278.
- ↑ Pollock, M.R., Torriani, A.-M. and Tridgell, E.G. (1956). „Crystalline bacterial penicillinase”. Biochem. J. 62: 387-391. PMID 13303985.
- ↑ Ross, G.W. and Boulton, M.G. (1973). „Purification of β-lactamases on QAE-sephadex”. Biochim. Biophys. Acta 309: 430-439. PMID 4731970.
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.
Литература
- Pollock, M.R. (1960). „Penicillinase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 4 (2nd izd.). New York: Academic Press. str. 269-278.
- Citri, N. (1971). „Penicillinase and other β-lactamases”. u: Boyer, P.D.. The Enzymes. 4 (3rd izd.). New York: Academic Press. str. 23-46.
Spoljašnje vezе
- MeSH Beta-lactamase
- 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