Enzymatic C-Acylation Data for Tetramate Antibiotic Diversification

Anfu Wei's dataset on figshare, last updated May 14, 2026, contains data related to enzymatic C-acylation for diversifying tetramate antibiotic scaffolds. The work identifies and characterizes a family of bacterial acyltransferases from species including Streptococcus macacae, Lactococcus hircilactis, Priestia megaterium, and Bacillus pseudomycoides. The 121.3 MB dataset likely contains experimental results on enzyme tolerance and the antibacterial activity of acylated products against methicillin-resistant Staphylococcus aureus.

Use Cases

• Training models to predict enzyme-substrate compatibility based on described broad tolerance toward tetramate acceptors and phenyl acyl ester donors.
• Analyzing structure-activity relationships for antibacterial compounds based on the described retained or improved activity against MRSA.
• Studying enzymatic C-C bond formation mechanisms in microbial natural product chemistry as described in the work.

Strengths

• Dataset size is 121.3 MB, indicating a medium-scale collection of data.
• The description provides specific details on the studied enzymes (SmaATase, LhATase, PmATase, BpATase) and their biological sources.
• Research context is clearly defined, focusing on enzymatic diversification of tetramate scaffolds beyond classical aromatic frameworks.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Description metadata is limited; actual data quality requires manual inspection after download.

Provenance

Source

Anfu Wei via figshare

Collection Method

Likely contains experimental data from the identification and characterization of bacterial acyltransferases.

Time Range

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Freshness

Last updated 2026-05-14 08:50:04; freshness should be verified.

Geography

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