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Structural analysis of zinc substitutions in the active site of thermolysin.
Native thermolysin binds a single catalytically essential zinc ion that is tetrahedrally coordinated by three protein ligands and a water molecule. During catalysis the zinc ligation is thought to change from fourfold to fivefold. Substitution of the active-site zinc with Cd2+, Mn2+, Fe2+, and Co2+...
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| Hoofdauteurs: | , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Cold Spring Harbor Laboratory Press
1995
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2142975/ https://ncbi.nlm.nih.gov/pubmed/8535232 |
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