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An Uncleavable Procaspase-3 Mutant Has a Lower Catalytic Efficiency but an Active Site Similar to That of Mature Caspase-3
We have examined the enzymatic activity of an uncleavable procaspase-3 mutant (D9A/D28A/D175A), which contains the wild-type catalytic residues in the active site. The results are compared to those for the mature caspase-3. Although at pH 7.5 and 25 °C the K(m) values are similar, the catalytic effi...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2003
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3119717/ https://ncbi.nlm.nih.gov/pubmed/14567691 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi034998x |
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