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
Functions
beta-lactamase activity
Processes
beta-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
ResourceLink
UniProtKB IDQ939N4
UniProtKB Entry NameQ939N4_ECOLX
General References
  1. 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]
  2. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB02772Sucroseapproved, experimental, investigationalunknownDetails
DB04035Ceftazidime BATSIexperimentalunknownDetails
DB09060AvibactamapprovedyesinhibitorDetails
DB12107Vaborbactamapproved, investigationalyesinhibitorDetails
DB12377Relebactamapproved, investigationalyesinhibitorDetails
DB01598ImipenemapprovednosubstrateDetails