An efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli.
High-level expression of the regulatory enzyme threonine deaminase in Escherichia coli strains grown on minimal medium that are deficient in the activities of enzymes needed for branched-chain amino acid biosynthesis result in growth inhibition, possibly because of the accumulation of toxic levels o...
Uloženo v:
| Vydáno v: | J Bacteriol |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1993
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC206772/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8407838/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.175.20.6605-6613.1993 |
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