| IED ID | IndEnz0010000711 |
| Enzyme Type ID | esterase000711 |
| Protein Name |
Metallo-beta-lactamase type 2 EC 3.5.2.6 B2 metallo-beta-lactamase Beta-lactamase type II Metallo-beta-lactamase NDM-1 Metallo-beta-lactamase type II New Delhi metallo-beta-lactamase-1 NDM-1 |
| Gene Name | blaNDM-1 |
| Organism | Klebsiella pneumoniae |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Klebsiella/Raoultella group Klebsiella Klebsiella pneumoniae |
| Enzyme Sequence | MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR |
| Enzyme Length | 270 |
| Uniprot Accession Number | C7C422 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibits by captopril, thiorphan, dimercaprol and tiopronin (PubMed:25815530). This enzyme is not susceptible to inactivation by the beta-lactamase-blocking agents clavulanic acid (PubMed:19770275). {ECO:0000269|PubMed:19770275, ECO:0000269|PubMed:25815530}. |
| Binding Site | BINDING 211; /note=Substrate; /evidence=ECO:0000269|PubMed:22713171; BINDING 220; /note=Substrate; via amide nitrogen; /evidence=ECO:0000269|PubMed:22713171 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:19770275}; |
| DNA Binding | |
| EC Number | 3.5.2.6 |
| Enzyme Function | FUNCTION: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin. {ECO:0000269|PubMed:19770275}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Binding site (2); Chain (1); Helix (9); Metal binding (6); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Antibiotic resistance;Hydrolase;Metal-binding;Periplasm;Plasmid;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (99) |
| Cross Reference PDB | 3PG4; 3RKJ; 3RKK; 3SBL; 3SFP; 3SPU; 3SRX; 3ZR9; 4EXS; 4EXY; 4EY2; 4EYB; 4EYF; 4EYL; 4GYQ; 4GYU; 4H0D; 4HKY; 4HL1; 4HL2; 4RAM; 4RAW; 4RBS; 4RL0; 4RL2; 4RM5; 4U4L; 5A5Z; 5JQJ; 5K4M; 5N0H; 5N0I; 5NBK; 5O2E; 5O2F; 5WIG; 5XP6; 5XP9; 5ZGE; 5ZGF; 5ZGI; 5ZGP; 5ZGQ; 5ZGR; 5ZGT; 5ZGU; 5ZGV; 5ZGW; 5ZGX; 5ZGY; 5ZGZ; 5ZH1; 5ZIO; 5ZJ1; 5ZJ2; 5ZJ7; 5ZJ8; 5ZJC; 6C6I; 6CAC; 6D1A; 6D1B; 6D1C; 6D1D; 6D1E; 6D1F; 6D1G; 6D1H; 6D1I; 6D1J; 6D1K; 6EFJ; 6EX7; 6IBS; 6IBV; 6JKB; 6LHE; 6LIP; 6LIZ; 6LJ0; 6LJ1; 6LJ2; 6LJ4; 6LJ5; 6LJ6; 6LJ7; 6LJ8; 6MDU; 6MGY; 6MGZ; 6NY7; 6O3R; 6Q2Y; 6Q30; 6RMF; 6TWT; 6V1M; 6ZYP; 6ZYQ; |
| Mapped Pubmed ID | 21507902; 21774017; 21931780; 22102018; 23363572; 25268575; 28965402; 29382822; 30150473; 30348667; 30466711; 30942078; 30996812; 31454231; 31483651; 32150407; 32353499; 33067430; 33302045; 34164056; 34853284; |
| Motif | |
| Gene Encoded By | Plasmid pKpANDM-1 |
| Mass | 28,499 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for cefuroxime {ECO:0000269|PubMed:19770275}; KM=10 uM for cefotaxime {ECO:0000269|PubMed:19770275}; KM=10 uM for cephalothin {ECO:0000269|PubMed:19770275}; KM=12 uM for piperacillin {ECO:0000269|PubMed:19770275}; KM=16 uM for penicillin G {ECO:0000269|PubMed:19770275}; KM=22 uM for ampicillin {ECO:0000269|PubMed:19770275}; KM=49 uM for cefoxitin {ECO:0000269|PubMed:19770275}; KM=49 uM for meropenem {ECO:0000269|PubMed:19770275}; KM=77 uM for cefepime {ECO:0000269|PubMed:19770275}; KM=94 uM for imipenem {ECO:0000269|PubMed:19770275}; KM=181 uM for ceftazidime {ECO:0000269|PubMed:19770275}; Note=No activity detected against the monobactam aztreonam. {ECO:0000269|PubMed:19770275}; |
| Metal Binding | METAL 120; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530"; METAL 122; /note="Zinc 1; via pros nitrogen"; /evidence="ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530"; METAL 124; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530"; METAL 189; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530"; METAL 208; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530"; METAL 250; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530" |
| Rhea ID | RHEA:20401 |
| Cross Reference Brenda | 3.5.2.6; |