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D-Ala-D-Ala dipeptidaza
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
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

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

\rightleftharpoons

2 D-Ala

Ovaj enzim je zavistan od Zn²⁺ jona.

Reference

↑ 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

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.

Vanjske veze

MeSH D-Ala-D-Ala+dipeptidase

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

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