| DOI | Resolve DOI: https://doi.org/10.1002/(SICI)1097-0134(19990801)36:2<238::AID-PROT9>3.0.CO;2-K |
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| Author | Search for: Munier-Lehmann, Hélène; Search for: Burlacu-Miron, Simona; Search for: Craescu, Constantin T.; Search for: Mantsch, Henry H.1 ; Search for: Schultz, Christian P.1 |
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| Name affiliation | - National Research Council Canada. NRC Institute for Biodiagnostics
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| Format | Text |
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| Type | Article |
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| Journal title | Proteins: Structure, Function, and Bioinformatics |
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| ISSN | 1097-0134 |
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| Volume | 36 |
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| Issue | 2 |
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| Pages | 238–248 |
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| Subject | adenylate kinase; short variant; Mycobacterium tuberculosis; NMR spectroscopy; infrared spectroscopy |
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| Abstract | The adk gene from Mycobacterium tuberculosis codes for an enzyme of 181 amino acids. A sequence comparison with 52 different forms of adenylate kinases (AK) suggests that the enzyme from M. tuberculosis belongs to a new subfamily of “short” bacterial AKs. The recombinant protein, overexpressed in Escherichia coli, exhibits a low catalytic activity and an unexpectedly high thermal stability (Tm = 64.8°C). Based on various spectroscopic data, on the known three-dimensional structure of the AK from E. coli and on secondary structure predictions for various sequenced AKs, we propose a structural model for AK from M. tuberculosis (AKmt). |
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| Publication date | 1999-08-01 |
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| Publisher | Wiley-Liss, Inc. |
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| Terms of use | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 23000809 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction |
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Record identifier | dc2407be-ee1f-4967-95bc-9e7968f26887 | | Record created | 2016-10-12 |
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| Record modified | 2016-10-12 |
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