MboA/MboB: Structural and Functional Data for an Acetylenase Enzyme

Edward D. Badding published data on the discovery of the MboA enzyme and its redox partner MboB in the mangotoxin biosynthetic operon. The dataset, last updated on 2026-04-28, includes findings that MboA catalyzes alkyne formation via iterative desaturations and reveals an unexpectedly short Fe–Fe distance in its crystal structure. The 8.1 MB dataset is available in TXT format under a CC-BY-NC-4.0 license.

Use Cases

• Studying the catalytic mechanism of alkyne formation based on the described iterative desaturation activity.
• Analyzing the structural basis for strong C–H bond activation based on the short Fe–Fe distance revealed in the crystal structure.
• Bioinformatics exploration of unannotated HDOs within biosynthetic operons, as demonstrated by the discovery approach.
• Investigating the gating role of dedicated redox partners like MboB in enzymatic transformations between alkene and alkyne.

Strengths

• Dataset includes specific structural data, such as the short Fe–Fe distance in the Fe(II)2-MboA crystal structure.
• The description provides a clear biological context, identifying the enzyme MboA, its partner MboB, and their role in the mangotoxin operon.
• File size is precisely documented as 8.1 MB.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment for quantitative analysis.
• The dataset is a single 8.1 MB text file, which may limit the scale of analysis.

Provenance

Source

figshare

Collection Method

Likely contains data generated from bioinformatics analysis, enzymatic assays, and X-ray crystallography as described.

Freshness

Last updated 2026-04-28 20:45:27; freshness should be verified.