| DOI | Resolve DOI: https://doi.org/10.1021/bi00127a002 |
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| Author | Search for: Glaser, Philippe; Search for: Presecan, Elena; Search for: Delepierre, Muriel; Search for: Surewicz, Witold K.1; Search for: Mantsch, Henry H.2; Search for: Bârzu, Octavian; Search for: Gilles, Anne-Marie |
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| Affiliation | - National Research Council Canada. NRC Institute for Biological Sciences
- National Research Council Canada. NRC Institute for Biodiagnostics
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| Format | Text, Article |
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| Abstract | The adk gene from Bacillus stearothermophilus was cloned and overexpressed in Escherichia coli under the control of the lac promoter. The primary structure of B. stearothermophilus adenylate kinase exhibited 76% identity with the enzyme from Bacillus subtilis, 60% identity with the enzyme from Lactococcus lactis, and 42% identity with the enzyme from E. coli. The most striking property of the adenylate kinase from B. stearothermophilus is the presence of a structural zinc atom bound to four cysteines in a zinc finger-like fashion. The ability to coordinate zinc is predicted also for a number of other isoforms of bacterial adenylate kinases. Furthermore, the tightly bound metal ion contributes to the high thermodynamic stability of adenylate kinase from B. stearothermophilus. |
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| Publication date | 1992 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRC-IBD-29 |
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| NPARC number | 9148462 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 27255db2-03c3-4f41-bb98-8a05aa95b895 |
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| Record created | 2009-06-25 |
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| Record modified | 2020-04-24 |
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