Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui
In: Biochemistry (Easton), Jg. 32 (1993), Heft 16, S. 4308-4313
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academicJournal
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Zugriff:
The gene coding for the enzyme malate dehydrogenase (MDH) of the extremely halophilic archaebacterium Haloarcula marismortui was isolated and sequenced. The enzyme is composed of 303 amino acids, and its molecular mass is 32 638 Da. The deduced amino acid sequence of the enzyme was found to be more similar to the sequence of L-lactate dehydrogenase (L-LDH) from various sources than to the sequence of other MDHs. The structural gene was cloned in the Escherichia coli expression vector pET11a, and large amounts of a soluble but inactive form of the enzyme were produced upon its induction. Activation of the enzyme was obtained by increasing the salt concentration to 3 M NaCl.
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Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui
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Autor/in / Beteiligte Person: | CENDRIN, F ; CHROBOCZEK, J ; ZACCAI, G ; EISENBERG, H ; MEVARECH, M |
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Zeitschrift: | Biochemistry (Easton), Jg. 32 (1993), Heft 16, S. 4308-4313 |
Veröffentlichung: | Washington, DC: American Chemical Society, 1993 |
Medientyp: | academicJournal |
Umfang: | print, 39 ref |
ISSN: | 0006-2960 (print) |
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