Identifying the catalytic residue of the ATPase reaction of DNA gyrase.
We propose a mechanism for the hydrolysis of ATP by the DNA gyrase B protein in which Glu42 acts as a general base and His38 has a role in aligning and polarizing the glutamate residue. We have tested this mechanism by site-directed mutagenesis, converting Glu42 to Ala, Asp, and Gln, and His38 to Al...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1993
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC47956/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8248233/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.90.23.11232 |
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