Beta-laktamaza

Beta-laktamaza
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
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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 {\displaystyle \rightleftharpoons } supstituisana beta-aminokiselina

Ova grupa enzima ima promenljivu specifičnost hidrolize beta-laktama.

Reference

  1. Citri, N. (1971). „Penicillinase and other β-lactamases”. u: Boyer, P.D.. The Enzymes. 4 (3rd izd.). New York: Academic Press. str. 23-46. 
  2. 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. 
  3. Kuwabara, S. (1970). „Purification and properties of two extracellular β-lactamases from Bacillus cereus 569-H”. Biochem. J. 118: 457-465. PMID 4990588. 
  4. 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. 
  5. Pollock, M.R., Torriani, A.-M. and Tridgell, E.G. (1956). „Crystalline bacterial penicillinase”. Biochem. J. 62: 387-391. PMID 13303985. 
  6. 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

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TemeTipovi
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