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Differences in malate dehydrogenases from the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium Moritella sp. strain 5710
- Source :
-
FEMS Microbiology Letters . Apr2004, Vol. 233 Issue 1, p165. 8p. - Publication Year :
- 2004
-
Abstract
- The gene encoding malate dehydrogenase (MDH) of the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 was cloned and sequenced. There were two positions [close to the active site (Ala-180) and in the subunit interaction site (His-229)] with 2D2-specific substitutions. The MDH genes of strain 2D2 and a psychrophilic bacterium Moritella sp. strain 5710 exhibiting the highest sequence similarity were overexpressed in Escherichia coli. The 2D2 MDH was more heat-stable than the 5710 MDH. The apparent <f>Km</f> value at 62.1 MPa for NADH of the 2D2 MDH was higher than that of the 5710 MDH. The 2D2 MDH in which a His–Gln substitution was introduced at position 229 decreased the thermal stability and <f>Km</f> value at 62.1 MPa. The 5710 MDH that was substituted Gln-229 with His increased the thermal stability and <f>Km</f> value at 62.1 MPa. These results indicate that the His residue at position 229 of the 2D2 MDH may play a role in the thermal stability and the MDH function at high pressure. [Copyright &y& Elsevier]
- Subjects :
- *BACTERIA
*DEHYDROGENASES
*ESCHERICHIA coli
*ESCHERICHIA
Subjects
Details
- Language :
- English
- ISSN :
- 03781097
- Volume :
- 233
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- FEMS Microbiology Letters
- Publication Type :
- Academic Journal
- Accession number :
- 12575556
- Full Text :
- https://doi.org/10.1016/j.femsle.2004.02.004