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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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Dades bibliogràfiques
Publicat a:Proc Natl Acad Sci U S A
Autors principals: Straus, D, Raines, R, Kawashima, E, Knowles, J R, Gilbert, W
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 1985
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Accés en línia: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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