D-Ala-D-Ala dipeptidase

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D-Ala-D-Ala dipeptidase
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EC no. 3.4.13.22
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D-Ala-D-Ala dipeptidase (EC 3.4.13.22, D-alanyl-D-alanine dipeptidase, vanX D-Ala-D-Ala dipeptidase, VanX) is an enzyme. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

D-Ala-D-Ala + H2O 2 D-Ala

This enzyme is Zn2+-dependent.

Related Research Articles

<span class="mw-page-title-main">Beta-lactam antibiotics</span> Class of broad-spectrum antibiotics

β-lactam antibiotics are antibiotics that contain a beta-lactam ring in their chemical structure. This includes penicillin derivatives (penams), cephalosporins and cephamycins (cephems), monobactams, carbapenems and carbacephems. Most β-lactam antibiotics work by inhibiting cell wall biosynthesis in the bacterial organism and are the most widely used group of antibiotics. Until 2003, when measured by sales, more than half of all commercially available antibiotics in use were β-lactam compounds. The first β-lactam antibiotic discovered, penicillin, was isolated from a strain of Penicillium rubens.

<span class="mw-page-title-main">Vancomycin</span> Pharmaceutical drug

Vancomycin is a glycopeptide antibiotic medication used to treat a number of bacterial infections. It is used intravenously as a treatment for complicated skin infections, bloodstream infections, endocarditis, bone and joint infections, and meningitis caused by methicillin-resistant Staphylococcus aureus. Blood levels may be measured to determine the correct dose. Vancomycin is also taken orally as a treatment for severe Clostridium difficile colitis. When taken orally it is poorly absorbed.

<span class="mw-page-title-main">DD-transpeptidase</span>

DD-transpeptidase is a bacterial enzyme that catalyzes the transfer of the R-L-αα-D-alanyl moiety of R-L-αα-D-alanyl-D-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor. It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands.

<span class="mw-page-title-main">Molecular recognition</span> Type of non-covalent bonding

The term molecular recognition refers to the specific interaction between two or more molecules through noncovalent bonding such as hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, π-π interactions, halogen bonding, or resonant interaction effects. In addition to these direct interactions, solvents can play a dominant indirect role in driving molecular recognition in solution. The host and guest involved in molecular recognition exhibit molecular complementarity. Exceptions are molecular containers, including e.g. nanotubes, in which portals essentially control selectivity.

Vancomycin-resistant <i>Enterococcus</i> Bacterial strains of Enterococcus that are resistant to the antibiotic vancomycin

Vancomycin-resistant Enterococcus, or vancomycin-resistant enterococci (VRE), are bacterial strains of the genus Enterococcus that are resistant to the antibiotic vancomycin.

<i>Enterococcus faecalis</i> Species of bacterium

Enterococcus faecalis – formerly classified as part of the group D Streptococcus system – is a Gram-positive, commensal bacterium inhabiting the gastrointestinal tracts of humans. Like other species in the genus Enterococcus, E. faecalis is found in healthy humans and can be used as a probiotic. The probiotic strains such as Symbioflor1 and EF-2001 are characterized by the lack of specific genes related to drug resistance and pathogenesis. As an opportunistic pathogen, E. faecalis can cause life-threatening infections, especially in the nosocomial (hospital) environment, where the naturally high levels of antibiotic resistance found in E. faecalis contribute to its pathogenicity. E. faecalis has been frequently found in reinfected, root canal-treated teeth in prevalence values ranging from 30% to 90% of the cases. Re-infected root canal-treated teeth are about nine times more likely to harbor E. faecalis than cases of primary infections.

<span class="mw-page-title-main">Penicillin-binding proteins</span> Class of proteins

Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases.

Cytosol alanyl aminopeptidase is an enzyme.

<span class="mw-page-title-main">Alanine racemase</span>

In enzymology, an alanine racemase is an enzyme that catalyzes the chemical reaction

In enzymology, an alanine—tRNA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">D-alanine—D-alanine ligase</span> Enzyme belonging to the ligase family

In enzymology, a D-alanine—D-alanine ligase is an enzyme that catalyzes the chemical reaction

Enterococcus gallinarum is a species of Enterococcus. E. gallinarum demonstrates an inherent, low-level resistance to vancomycin. Resistance is due to a chromosomal gene, vanC, which encodes for a terminal D-alanine-D-serine instead of the usual D-alanine-D-alanine in cell wall peptidoglycan precursor proteins. That is a separate mechanism than the vancomycin resistance seen in VRE isolates of E. faecium and E. faecalis which is mediated by vanA or vanB. This species is known to cause clusters of infection, although it considered very rare. It is the only other known enterococcal species besides E. faecium and E. faecalis known to cause outbreaks and spread in hospitals.

In molecular biology, VanY are protein domains found in enzymes named metallopeptidases. They are vital to bacterial cell wall synthesis and antibiotic resistance.

Lipid II:glycine glycyltransferase (EC 2.3.2.16, N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase, femX (gene)) is an enzyme with systematic name alanyl-D-alanine-diphospho-ditrans, octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase. This enzyme catalyses the following chemical reaction

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.17, femA (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase. This enzyme catalyses the following chemical reaction

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.18, femB (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase. This enzyme catalyses the following chemical reaction

Xaa-methyl-His dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. This enzyme catalyses the following chemical reaction

D-alanine—(R)-lactate ligase (EC 6.1.2.1, VanA, VanB, VanD) is an enzyme with systematic name D-alanine:(R)-lactate ligase (ADP-forming). This enzyme catalyses the following chemical reaction

D-Alanine—D-serine ligase is an enzyme with systematic name D-alanine:D-serine ligase (ADP-forming). This enzyme catalyses the following chemical reaction

References

  1. ↑ Reynolds PE, Depardieu F, Dutka-Malen S, Arthur M, Courvalin P (September 1994). "Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine". Molecular Microbiology. 13 (6): 1065–70. doi:10.1111/j.1365-2958.1994.tb00497.x. PMID   7854121.
  2. ↑ Wu Z, Wright GD, Walsh CT (February 1995). "Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147". Biochemistry. 34 (8): 2455–63. doi:10.1021/bi00008a008. PMID   7873524.
  3. ↑ McCafferty DG, Lessard IA, Walsh CT (August 1997). "Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX". Biochemistry. 36 (34): 10498–505. doi:10.1021/bi970543u. PMID   9265630.
  4. ↑ Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH (July 1998). "The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance". Molecular Cell. 2 (1): 75–84. doi: 10.1016/s1097-2765(00)80115-x . PMID   9702193.
  5. ↑ Tan AL, Loke P, Sim TS (2002). "Molecular cloning and functional characterisation of VanX, a D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2)". Research in Microbiology. 153 (1): 27–32. doi:10.1016/s0923-2508(01)01282-7. PMID   11881895.
  6. ↑ Matthews ML, Periyannan G, Hajdin C, Sidgel TK, Bennett B, Crowder MW (October 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". Journal of the American Chemical Society. 128 (40): 13050–1. doi:10.1021/ja0627343. PMC   2547881 . PMID   17017774.
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