Beta-lactamase
Details
- Name
- Beta-lactamase
- Synonyms
- 3.5.2.6
- Gene Name
- Not Available
- Organism
- Escherichia coli
- Amino acid sequence
>lcl|BSEQ0052131|Beta-lactamase MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQ VLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTM TLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTAGDKTGS GGYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL
- Number of residues
- 291
- Molecular Weight
- 30893.0
- Theoretical pI
- Not Available
- GO Classification
- Functionsbeta-lactamase activityProcessesbeta-lactam antibiotic catabolic process / response to antibiotic
- General Function
- Not Available
- Specific Function
- Beta-lactamase activity
- Pfam Domain Function
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q939N4 UniProtKB Entry Name Q939N4_ECOLX - General References
- Bonnet R, Dutour C, Sampaio JL, Chanal C, Sirot D, Labia R, De Champs C, Sirot J: Novel cefotaximase (CTX-M-16) with increased catalytic efficiency due to substitution Asp-240-->Gly. Antimicrob Agents Chemother. 2001 Aug;45(8):2269-75. doi: 10.1128/AAC.45.8.2269-2275.2001. [Article]
- Chen Y, Delmas J, Sirot J, Shoichet B, Bonnet R: Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability. J Mol Biol. 2005 Apr 29;348(2):349-62. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02772 Sucrose approved, experimental, investigational unknown Details DB04035 Ceftazidime BATSI experimental unknown Details DB09060 Avibactam approved yes inhibitor Details DB12107 Vaborbactam approved, investigational yes inhibitor Details DB12377 Relebactam approved, investigational yes inhibitor Details DB01598 Imipenem approved no substrate Details