Modulation of the allosteric equilibrium of yeast chorismate mutase by variation of a single amino acid residue.
Chorismate mutase (EC 5.4.99.5) from the yeast Saccharomyces cerevisiae is an allosteric enzyme which can be locked in its active R (relaxed) state by a single threonine-to-isoleucine exchange at position 226. Seven new replacements of residue 226 reveal that this position is able to direct the enzy...
Uloženo v:
| Vydáno v: | J Bacteriol |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1995
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC176788/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7883726/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.177.6.1645-1648.1995 |
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