| IED ID | IndEnz0002010289 |
| Enzyme Type ID | protease010289 |
| Protein Name |
D-alanyl-D-alanine dipeptidase D-Ala-D-Ala dipeptidase EC 3.4.13.22 Vancomycin B-type resistance protein VanX |
| Gene Name | vanX |
| Organism | Enterococcus faecium (Streptococcus faecium) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecium (Streptococcus faecium) |
| Enzyme Sequence | MEIGFTFLDEIVHGVRWDAKYATWDNFTGKPVDGYEVNRIVGTYELAESLLKAKELAATQGYGLLLWDGYRPKRAVNCFMQWAAQPENNLTKESYYPNIDRTEMISKGYVASKSSHSRGSAIDLTLYRLDTGELVPMGSRFDFMDERSHHAANGISCNEAQNRRRLRSIMENSGFEAYSLEWWHYVLRDEPYPNSYFDFPVK |
| Enzyme Length | 202 |
| Uniprot Accession Number | Q06241 |
| Absorption | |
| Active Site | ACT_SITE 181; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:9702193 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by aminoalkyl phosphinate analogs. {ECO:0000269|PubMed:7873524}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine; Xref=Rhea:RHEA:20661, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822; EC=3.4.13.22; Evidence={ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:7854121, ECO:0000269|PubMed:7873524}; |
| DNA Binding | |
| EC Number | 3.4.13.22 |
| Enzyme Function | FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. {ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:7854121, ECO:0000269|PubMed:7873524}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9. {ECO:0000269|PubMed:7873524}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Helix (9); Metal binding (3); Site (1); Turn (2) |
| Keywords | 3D-structure;Antibiotic resistance;Cell wall biogenesis/degradation;Dipeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Plasmid;Protease;Zinc |
| Interact With | |
| Induction | INDUCTION: By vancomycin, mediated by VanS/VanR. {ECO:0000269|PubMed:1556077}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1R44; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pIP816 |
| Mass | 23,380 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for D-Ala-D-Ala (in the absence of divalent cations) {ECO:0000269|PubMed:7873524}; KM=2.8 mM for D-Ala-D-Ser {ECO:0000269|PubMed:7873524}; KM=1.7 mM for D-Ser-D-Ala {ECO:0000269|PubMed:7873524}; Vmax=12.3 nmol/min/ug enzyme with D-Ala-D-Ala as substrate {ECO:0000269|PubMed:7873524}; Vmax=4.7 nmol/min/ug enzyme with D-Ala-D-Ser as substrate {ECO:0000269|PubMed:7873524}; Vmax=1.3 nmol/min/ug enzyme with D-Ser-D-Ala as substrate {ECO:0000269|PubMed:7873524}; Note=kcat is 4.7 sec(-1) with D-Ala-D-Ala. kcat is 1.8 sec(-1) with D-Ala-D-Ser. kcat is 0.35 sec(-1) with D-Ser-D-Ala. kcat is 0.005 sec(-1) with D-Ala-D-lactate.; |
| Metal Binding | METAL 116; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9702193"; METAL 123; /note="Zinc; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9702193"; METAL 184; /note="Zinc; via pros nitrogen; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9702193" |
| Rhea ID | RHEA:20661 |
| Cross Reference Brenda | 3.4.13.22; |