Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme.
We have replaced the glutamic acid-165 at the active site of chicken triosephosphate isomerase with an aspartic acid residue using site-directed mutagenesis. Expression of the mutant protein in a strain of Escherichia coli that lacks the bacterial isomerase results in a complementation phenotype tha...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1985
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC397539/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3887397/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.82.8.2272 |
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