Beta-lactamase
Details
- Name
- Beta-lactamase
- Kind
- protein
- Synonyms
- 3.5.2.6
- bla IMP
- bla-imp
- blaESP
- imp
- Gene Name
- blaIMP-1
- UniProtKB Entry
- Q79MP6TrEMBL
- Organism
- Pseudomonas aeruginosa
- NCBI Taxonomy ID
- 287
- Amino acid sequence
>lcl|BSEQ0019484|Beta-lactamase MSKLSVFFIFLFCSIATAAESLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNA EAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELT NELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKP YGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKGLNESKK PSKPSN
- Number of residues
- 246
- Molecular Weight
- 27119.985
- Theoretical pI
- 8.94
- GO Classification
- Functionsbeta-lactamase activity / zinc ion bindingProcessesantibiotic catabolic process / response to antibiotic
- General Function
- Not Available
- Specific Function
- beta-lactamase activity
- Pfam Domain Function
- Lactamase_B (PF00753)
- Signal Regions
- 1-18
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
- Not Available
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q79MP6 UniProtKB Entry Name Q79MP6_PSEAI GenBank Protein ID 27368096 GenBank Gene ID AY168635 PDB ID(s) 1DDK, 1JJE, 1JJT, 3WXC, 4F6H, 4F6Z - General References
- Concha NO, Janson CA, Rowling P, Pearson S, Cheever CA, Clarke BP, Lewis C, Galleni M, Frere JM, Payne DJ, Bateson JH, Abdel-Meguid SS: Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry. 2000 Apr 18;39(15):4288-98. [Article]
- Toney JH, Hammond GG, Fitzgerald PM, Sharma N, Balkovec JM, Rouen GP, Olson SH, Hammond ML, Greenlee ML, Gao YD: Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase. J Biol Chem. 2001 Aug 24;276(34):31913-8. Epub 2001 Jun 4. [Article]
- Horton LB, Shanker S, Mikulski R, Brown NG, Phillips KJ, Lykissa E, Venkataram Prasad BV, Palzkill T: Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-beta-lactamase active site. Antimicrob Agents Chemother. 2012 Nov;56(11):5667-77. doi: 10.1128/AAC.01276-12. Epub 2012 Aug 20. [Article]
- Hiraiwa Y, Saito J, Watanabe T, Yamada M, Morinaka A, Fukushima T, Kudo T: X-ray crystallographic analysis of IMP-1 metallo-beta-lactamase complexed with a 3-aminophthalic acid derivative, structure-based drug design, and synthesis of 3,6-disubstituted phthalic acid derivative inhibitors. Bioorg Med Chem Lett. 2014 Oct 15;24(20):4891-4. doi: 10.1016/j.bmcl.2014.08.039. Epub 2014 Sep 6. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2,3-Bis-Benzo[1,3]Dioxol-5-Ylmethyl-Succinic Acid experimental unknown target Details 2-Benzo[1,3]Dioxol-5-Ylmethyl-3-Benzyl-Succinic Acid experimental unknown target Details