Insights into specificity and catalytic mechanism of amphotericin B/nystatin thioesterase.

doi:10.1002/prot.26041

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Article

Insights into specificity and catalytic mechanism of amphotericin B/nystatin thioesterase.

Proteins - 1 May 2021

Wang Rufan, Tao Wentao, Liu Lei, Li Chen, Bai Linquan, Zhao Yi-Lei, Shi Ting

Abstract excerpt

Polyene polyketides amphotericin B (AMB) and nystatin (NYS) are important antifungal drugs. Thioesterases (TEs), located at the last module of PKS, control the release of polyketides by cyclization or hydrolysis. Intrigued by the tiny structural difference between AMB and NYS, as well as the high sequence identity between AMB TE and NYS TE, we constructed four systems to study the structural characteristics,...

Topics

Amphotericin B
Bacterial Proteins
Binding Sites
Biocatalysis
Catalytic Domain
Cyclization
Hydrogen Bonding
Hydrolysis
Hydrophobic and Hydrophilic Interactions
Isoenzymes
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Dynamics Simulation

Mutation

Nystatin

Protein Binding

Protein Conformation, alpha-Helical

Protein Conformation, beta-Strand

Source

Open in PubMed

Identifiers

PMID: 33389775
DOI: 10.1002/prot.26041

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