Thermolysin Peptide Binding Data from Crystallographic Analysis

Crystallographic analysis data of the binding interaction between the dipeptide L-valyl-L-tryptophan and the enzyme thermolysin. The study, authored by Hazel M. Holden from the University of Oregon, provides structural evidence for the enzyme's hydrolysis mechanism by detailing hydrogen bond distances and subsite occupancy. It directly supports a previously proposed mechanism of action for thermolysin and, by analogy, for carboxypeptidase A.

Use Cases

• Modeling enzyme active site interactions based on described hydrogen bond distances and subsite occupancy.
• Validating computational docking simulations for thermolysin inhibitors based on the crystallographic binding mode.
• Studying peptide hydrolysis product binding preferences as described for the S1'-S2' subsites.
• Comparing binding modes of different dipeptides like Val-Trp and Ala-Phe to understand enzyme specificity.

Strengths

• Data is derived from high-resolution crystallographic refinement, a precise experimental method.
• The description provides specific structural details, such as a 2.8 Å distance between a valyl amino group and Glu-143.

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 Oregon

Collection Method

Crystallographic analysis