MilM Dimerization: Biochemical and Simulation Data for PLP-Dependent Hydroxylation

Biochemical, biophysical, and molecular dynamics simulation data for the enzyme MilM from Streptoverticillium rimofaciens B-98891. The dataset supports findings on its dimerization-dependent catalytic mechanism for hydroxylating l-arginine during mildiomycin biosynthesis. It was authored by Simita Das and last updated on 2026-05-15.

Use Cases

• Modeling protein-protein interaction dynamics based on the described dimer-mediated alternating-lid mechanism
• Analyzing active-site residue contributions to catalysis based on site-directed mutagenesis data
• Studying substrate and cofactor stabilization networks in PLP-dependent oxidases/hydroxylases
• Investigating enzyme reaction mechanisms involving superoxide radical anion intermediates

Strengths

• Dataset includes multiple data types: biochemical, biophysical, structural modeling, and molecular dynamics simulations.
• Focuses on a specific, detailed catalytic mechanism for a PLP-dependent enzyme.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• The 10.7 MB size suggests a relatively small dataset.

Provenance

Source

Simita Das via figshare

Collection Method

Experimental and computational investigations including site-directed mutagenesis and MD simulations.

Freshness

Last updated 2026-05-15 08:04:13