Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus

التفاصيل البيبلوغرافية
العنوان: Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus
المؤلفون: Stefan Fabry, Thomas Niermann, Reinhard Hensel, Erika Honka, Peter Palm
المصدر: European Journal of Biochemistry. 188:623-632
بيانات النشر: Wiley, 1990.
سنة النشر: 1990
مصطلحات موضوعية: Molecular Sequence Data, Restriction Mapping, Dehydrogenase, Biochemistry, Malate dehydrogenase, Gene Expression Regulation, Enzymologic, Bacterial Proteins, Malate Dehydrogenase, Animals, Amino Acid Sequence, Amino Acids, Cloning, Molecular, Phylogeny, Bacteria, Base Sequence, L-Lactate Dehydrogenase, biology, Molecular mass, Thermophile, Temperature, Protein primary structure, Gene Expression Regulation, Bacterial, biology.organism_classification, Archaea, Enzyme Activation, Methanothermus, Kinetics, Genes, Bacterial, Methanothermus fervidus, NAD+ kinase
الوصف: L-Malate dehydrogenase from the extremely thermophilic mathanogen Methanothermus fervidus was isolated and its phenotypic properties were characterized. The primary structure of the protein was deduced from the coding gene. The enzyme is a homomeric dimer with a molecular mass of 70 kDa, possesses low specifity for NAD+ or NADP+ and catalyzes preferentially the reduction of oxalacetate. The temperature dependence of the activity as depicted in the Arrhenius and van't Hoff plots shows discontinuities near 52°C, as was found for glyceraldehyde-3-phosphate dehydrogenase from the same organism. With respect to the primary structure, the archaebacterial L-malate dehydrogenase deviates strikingly from the eubacterial and eukaryotic enzymes. The sequence similarity is even lower than that between the L-malate dehydrogenases and L-lactate dehydrogenases of eubacteria and eukaryotes. The phylogenetic meaning of this relationship is discussed.
تدمد: 1432-1033
0014-2956
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4009ce86afeac4e8b8b174f446b2b59Test
https://doi.org/10.1111/j.1432-1033.1990.tb15443.xTest
حقوق: CLOSED
رقم الانضمام: edsair.doi.dedup.....c4009ce86afeac4e8b8b174f446b2b59
قاعدة البيانات: OpenAIRE