Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mechanism and diversity of the erythromycin esterase family of enzymes.

Biochemistry - 28 Feb 2012

Morar Mariya, Pengelly Kate, Koteva Kalinka, Wright Gerard D

Abstract excerpt

Macrolide antibiotics such as azithromycin and erythromycin are mainstays of modern antibacterial chemotherapy, and like all antibiotics, they are vulnerable to resistance. One mechanism of macrolide resistance is via drug inactivation: enzymatic hydrolysis of the macrolactone ring catalyzed by erythromycin esterases, EreA and EreB. A genomic enzymology approach was taken to gain insight into the catalytic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carboxylic Ester Hydrolases
Share to Catalysis
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Bacterial

Share to Macrolides

Share to Pseudomonas

Share to Sequence Analysis, Protein

Share to Substrate Specificity

Source

Identifiers

PMID: 22303981
DOI: 10.1021/bi201790u

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism and diversity of the erythromycin esterase family of enzymes.PMID 22303981Read ↗

Hydration and hydrolysis define antibiotic resistance conferred by macrolide esterasesSemantic proximity Read ↗

Targeting Metallo-β-Lactamase Enzymes in Antibiotic ResistanceSemantic proximity Read ↗

Development of Genetically Encoded Biosensors for Reporting the Methyltransferase-Dependent Biosynthesis of Semisynthetic Macrolide AntibioticsSemantic proximity Read ↗

Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community.Semantic proximity Read ↗

Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily.Semantic proximity Read ↗

Clinical strain of Staphylococcus aureus inactivates and causes efflux of macrolidesSemantic proximity Read ↗

Engineering dynamic gates in binding pocket of penicillin G acylase to selectively degrade bacterial signaling moleculesSemantic proximity Read ↗

Unique structural and ligand binding properties of the <i>Staphylococcus aureus</i> serine hydrolase FphESemantic proximity Read ↗

Insights into erythromycin action from studies of its activity as inducer of resistance.Semantic proximity Read ↗

Re-characterization of mono-2-ethylhexyl phthalate hydrolase belonging to the serine hydrolase family.Semantic proximity Read ↗

Binuclear Metallohydrolases: Complex Mechanistic Strategies for a Simple Chemical ReactionSemantic proximity Read ↗

An Atypical α/β-Hydrolase Fold Revealed in the Crystal Structure of Pimeloyl-Acyl Carrier Protein Methyl Esterase BioG from Haemophilus influenzae.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.