MilM Enzyme Dimerization Data for PLP-Dependent Hydroxylation Mechanism

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

Use Cases

• Analyzing enzyme-substrate interactions based on molecular dynamics simulations described in the study
• Investigating the role of dimerization in catalysis based on the proposed alternating-lid mechanism
• Studying cofactor stabilization based on the identified key catalytic residues Lys232 and His31
• Modeling reaction pathways for PLP-dependent hydroxylation based on the described product and byproduct formation

Strengths

• Dataset includes detailed biochemical and biophysical investigations of a specific enzyme
• Findings are supported by structural modeling and molecular dynamics simulations
• License is CC-BY-NC-4.0, allowing for non-commercial reuse with attribution

Limitations

• Column-level documentation is absent; field semantics must be inferred after download
• Row count is unknown, which may limit suitability assessment
• Data size is 59.7 MB, indicating a relatively small dataset

Provenance

Source

figshare

Collection Method

Experimental results from biochemical assays, biophysical studies, structural modeling, and molecular dynamics simulations.

Freshness

Last updated 2026-05-15 08:04:17