CYP1232A24: Structure of a Cytochrome P450 Enzyme from Arthrobacter sp.

A dataset from the University of Stuttgart details the structure and function of cytochrome P450 enzymes from Arthrobacter sp. The research identifies two enzymes, CYP1232F1 and CYP1232A24, involved in the metabolic degradation of papaverine alkaloids. The dataset includes a crystal structure of CYP1232A24 and results from constructing a whole-cell biocatalyst that produced up to 1.77 g l-1 of a target compound.

Use Cases

• Analyzing enzyme-substrate specificity based on the reported crystal structure and demethylation activity.
• Engineering microbial biocatalysts based on the successful expression of CYP1232A24 in E. coli.
• Studying metabolic pathways for alkaloid degradation based on the identified roles of P450s in papaverine metabolism.
• Comparing P450 enzyme structures based on the low sequence identity (29%) to previously published structures.

Strengths

• Includes a crystal structure for CYP1232A24, enabling detailed mechanistic analysis.
• Reports quantitative biocatalyst performance, producing up to 1.77 g l-1 of 3,4-dihydroxyphenylacetic acid.
• Provides biochemical characterization of two enzymes with defined physiological roles.

Limitations

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

Provenance

Source

University of Stuttgart

Collection Method

Likely contains results from X-ray crystallography, phylogenetic analysis, genomic analysis, and biochemical assays.