MilM Enzyme Dimerization and Catalytic Mechanism Data

Biochemical, biophysical, and computational data on the MilM enzyme from Streptoverticillium rimofaciens B-98891. The dataset includes results from structural modeling, molecular dynamics simulations, and site-directed mutagenesis studies. It was authored by Simita Das and last updated on 2026-05-15.

Use Cases

• Modeling enzyme-substrate interactions based on the described active-site residue network.
• Simulating protein dynamics based on the described dimer-mediated alternating-lid mechanism.
• Analyzing catalytic pathways based on the described reaction products and intermediates.
• Studying cofactor stabilization based on the described roles of Lys232 and His31.

Strengths

• Includes data from multiple experimental techniques: biochemical assays, biophysical studies, structural modeling, and MD simulations.
• Focuses on a specific, well-defined enzyme (MilM) and its catalytic mechanism.
• Dataset size is 28.3 MB, indicating a substantial amount of supporting data.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.

Provenance

Source

figshare

Collection Method

Likely contains results from experimental and computational investigations described in the associated research.

Freshness

Last updated 2026-05-15 08:04:15; freshness should be verified.