| DOI | Trouver le DOI : https://doi.org/10.1002/(SICI)1097-0134(19990801)36:2<238::AID-PROT9>3.0.CO;2-K |
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| Auteur | Rechercher : Munier-Lehmann, Hélène; Rechercher : Burlacu-Miron, Simona; Rechercher : Craescu, Constantin T.; Rechercher : Mantsch, Henry H.1; Rechercher : Schultz, Christian P.1 |
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| Affiliation | - Conseil national de recherches du Canada. Institut du biodiagnostic du CNRC
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| Format | Texte, Article |
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| Sujet | adenylate kinase; short variant; Mycobacterium tuberculosis; NMR spectroscopy; infrared spectroscopy |
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| Résumé | 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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| Date de publication | 1999-08-01 |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Numéro NPARC | 23000809 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | dc2407be-ee1f-4967-95bc-9e7968f26887 |
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| Enregistrement créé | 2016-10-12 |
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| Enregistrement modifié | 2020-03-20 |
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