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Torleiv Lien - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate reducing bacterium desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
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Purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate‐reducing bacterium Desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
Ida Helene Steen - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate reducing bacterium desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
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Purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate‐reducing bacterium Desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
Hans Jörnvall - One of the best experts on this subject based on the ideXlab platform.
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The Alcohol Dehydrogenase System
Advances in experimental medicine and biology, 1995Co-Authors: Hans Jörnvall, Olle Danielsson, Lars Hjelmqvist, Bengt Persson, Jawed ShafqatAbstract:Alcohol Dehydrogenases of different types are common enzymes in nature. Two of these families, the medium-chain dehydrogenase/reductase family, MDR, and the shortchain dehydrogenase/reductase family, SDR, are well studied and known since long, but have experienced a recent “explosion” of new knowledge, extension and importance. The MDR family includes the classical zinc-containing liver alcohol Dehydrogenases encompassing the classes of human liver alcohol dehydrogenase, while the SDR family includes the Drosophila alcohol dehydrogenase, which has shorter subunits, no similar metal requirements, other sub-domain arrangements with different structural relationships, and other subunit interactions.
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Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a ‘variable’ enzyme ‘Variable’ and ‘constant’ enzymes within the alcohol and aldehyde dehydrogenase families
FEBS letters, 1991Co-Authors: Shih-jiun Yin, Nikolaos Vagelopoulos, Sung-ling Wang, Hans JörnvallAbstract:Stomach aldehyde dehydrogenase was structurally evaluated by analysis of peptide fragments of the human enzyme and comparisons with corresponding parts from other characterized aldehyde Dehydrogenases. The results establish a large part of the structure, confirming that the stomach enzyme is identical to the inducible or tumor-derived dimeric aldehyde dehydrogenase. In addition, species variations between identical sets of different aldehyde and alcohol Dehydrogenases reveal that stomach aldehyde dehydrogenase exhibits a fairly rapid rate of evolutionary changes, similar to that for the likewise ‘variable’ classical alcohol dehydrogenase, sorbitol dehydrogenase, and cytosolic aldehyde dehydrogenase but in contrast to the ‘constant’ class III alcohol dehydrogenase and mitochondrial aldehyde dehydrogenase. This establishes that rates of divergence in the aldehyde and alcohol Dehydrogenases are unrelated to subunit size or quaternary structure, highlights the unique nature of class III alcohol dehydrogenase, and positions the stomach aldehyde dehydrogenase in a group with more ordinary features.
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Pseudomonas 3β‐hydroxysteroid dehydrogenase
European journal of biochemistry, 1991Co-Authors: Shih-jiun Yin, Nikolaos Vagelopoulos, Gunilla Lundquist, Hans JörnvallAbstract:The 3β-hydroxysteroid dehydrogenase of Pseudomonas testosteroni commercially available was purified by an FPLC step and submitted to sequence determination by peptide analysis. The structure obtained reveals a 253-residue polypeptide chain, with an N-terminal, free α-amino group, and a low cysteine content. Comparisons with other hydroxysteroid Dehydrogenases recently characterized reveal distant similarities with prokaryotic and, to some extent, also eukaryotic forms of separate specificities. Residue identities with a Streptomyces 20β-hydroxysteroid dehydrogenase are 35% and distributed over the entire molecule, whereas residue identities with the mammalian 17β-hydroxysteroid dehydrogenase only constitute 20%, and are essentially limited to the N-terminal and central parts, Nevertheless, all these enzymes exhibit a conserved tyrosine residue (position 151 in the present enzyme) noted as possibly having a functional role in some members of this protein family. Combined, the results establish the prokaryotic 3β-hydroxysteroid dehydrogenase as belonging to the family of short-chain alcohol Dehydrogenases, reveal that the hydroxysteroid Dehydrogenases are no more closely related than Dehydrogenases with other enzyme activities within the family (e.g. glucose, ribitol, hydroxyprostaglandin Dehydrogenases), show several of the mammalian hydroxysteroid Dehydrogenases to have subunits of longer size with different patterns of similarity than those of the prokaryotic family members characterized, and define important segments of the coenzyme-binding region for this enzyme group.
Nils-kåre Birkeland - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate reducing bacterium desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
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Purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate‐reducing bacterium Desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
Marit Steine Madsen - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate reducing bacterium desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.
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Purification and characterization of a monomeric isocitrate dehydrogenase from the sulfate‐reducing bacterium Desulfobacter vibrioformis and demonstration of the presence of a monomeric enzyme in other bacteria
Fems Microbiology Letters, 1998Co-Authors: Ida Helene Steen, Nils-kåre Birkeland, Marit Steine Madsen, Torleiv LienAbstract:NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was purified to homogeneity from the sulfate-reducing bacterium Desulfobacter vibrioformis, and shown to be a monomeric protein with a molecular mass of 80 kDa. The pH and temperature optima were 8.5 and 45°C, respectively. The N-terminal amino acid sequence (Thr, Glu, Thr, Ile, Arg, Trp, Thr, X, Thr, Asp, Glu, Ala, Pro, Leu, Leu, Ala, Thr) showed similarity with that of other known monomeric isocitrate Dehydrogenases. Catalytically active isocitrate dehydrogenase from D. vibrioformis was obtained by activity staining after SDS-PAGE and removal of SDS from the gel. This technique revealed a NADP+-dependent monomeric enzyme in other Desulfobacter spp., Desulfuromonas acetoxidans and Chlorobium tepidium. These findings imply that monomeric isocitrate Dehydrogenases are present in distantly related bacteria and indicate an early evolution of monomeric isocitrate Dehydrogenases in the bacterial lineage.