InterPro domain: IPR007815

This entry contains erythromycin esterase, which shares conserved active site residues of the Tiki/TraB family. Erythromycin esterases (EreA and EreB) disrupt erythromycin via the hydrolysis of the macrolactone ring. A critical catalytic histidine acts as a general base in the activation of a water molecule. Macrolides act by inhibiting bacterial protein synthesis by binding at the exit tunnel of ribosomal subunit 50s, blocking the translation of the polypeptide. Erythromycin esterase, typically found in integrons and transposons, confers antibiotic resistance through the disruption of the drug ring structure. EreB substrate profile is substantially broader than that for EreA, being able to also metabolize semisynthetic derivatives such as azalide azithromycin [ 1 , 2 , 3 , 4 , 5 ].

1. Mechanism and diversity of the erythromycin esterase family of enzymes. Biochemistry 51, 1740-51
2. Analysis of the nucleotide sequence of the ereB gene encoding the erythromycin esterase type II. Nucleic Acids Res. 14, 4987-99
3. Origin and evolution of genes specifying resistance to macrolide, lincosamide and streptogramin antibiotics: data and hypotheses. J Antimicrob Chemother 20, 783-802
4. Nucleotide sequence of the gene ereA encoding the erythromycin esterase in Escherichia coli. Gene 35, 271-8
5. Cofacial heme binding is linked to dimerization by a bacterial heme transport protein. J. Mol. Biol. 362, 1108-19