D-Ala-D-Ala dipeptidaza
(Preusmjereno sa stranice D-Ala-D-Ala-dipeptidaza)
D-Ala-D-Ala dipeptidaza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.4.13.22 | ||||||||
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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D-Ala-D-Ala dipeptidaza (EC 3.4.13.22, D-alanil-D-alanin dipeptidaza, vanX D-Ala-D-Ala dipeptidaza, VanX) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- D-Ala-D-Ala + H2O 2 D-Ala
Ovaj enzim je zavistan od Zn2+ jona.
Reference[uredi | uredi kod]
- ↑ Reynolds, P.E., Depardieu, F., Dutka-Malen, S., Arthur, M. and Courvalin, P. (1994). „Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine”. Mol. Microbiol. 13: 1065-1070. PMID 7854121.
- ↑ Wu, Z., Wright, G.D. and Walsh, C.T. (1995). „Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147”. Biochemistry 34: 2455-2463. PMID 7873524.
- ↑ McCafferty, D.G., Lessard, I.A. and Walsh, C.T. (1997). „Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX”. Biochemistry 36: 10498-10505. PMID 9265630.
- ↑ Bussiere, D.E., Pratt, S.D., Katz, L., Severin, J.M., Holzman, T. and Park, C.H. (1998). „The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance”. Mol. Cell. 2: 75-84. PMID 9702193.
- ↑ Tan, A.L., Loke, P. and Sim, T.S. (2002). „Molecular cloning and functional characterisation of VanX, a D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2)”. Res. Microbiol. 153: 27-32. PMID 11881895.
- ↑ Matthews, M.L., Periyannan, G., Hajdin, C., Sidgel, T.K., Bennett, B. and Crowder, M.W. (2006). „Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid-freeze quench EPR studies on the Co(II)-substituted enzyme”. J. Am. Chem. Soc. 128: 13050-13051. PMID 17017774.
Literatura[uredi | uredi kod]
- 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.