Biomaterial Database

Purification and characterization of the formate dehydrogenase from Desulfovibrio vulgaris Hildenborough. 1995

C Sebban, and L Blanchard, and M Bruschi, and F Guerlesquin

Unité de Bioénergétique et Ingénierie des Protéines, IFRC1, CNRS, Marseille, France.

Formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, a sulfate-reducing bacterium, has been isolated and characterized. The enzyme is composed of three subunits. A high molecular mass subunit (83,500 Da) is proposed to contain a molybdenum cofactor, a 27,000 Da subunit is found to be similar to the Fe-S subunit of the formate dehydrogenase from Escherichia coli and a low molecular mass subunit (14,000 Da) holds a c-type heme. The presence of heme c in formate dehydrogenase is reported for the first time and is correlated to the peculiar low oxidoreduction potential of the metabolism of these strictly anaerobic bacteria. In vitro measurements have shown that a monoheme cytochrome probably acts as a physiological partner of the enzyme in the periplasm.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D002451	Cell Compartmentation	A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.	Cell Compartmentations,Compartmentation, Cell,Compartmentations, Cell
D003067	Coenzymes	Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.	Coenzyme,Enzyme Cofactor,Cofactors, Enzyme,Enzyme Cofactors,Cofactor, Enzyme
D005560	Formate Dehydrogenases	Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.	Formate Dehydrogenase,Formate Hydrogenlyases,NAD-Formate Dehydrogenase,Dehydrogenase, Formate,Dehydrogenase, NAD-Formate,Dehydrogenases, Formate,Hydrogenlyases, Formate,NAD Formate Dehydrogenase
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D016969	Desulfovibrio vulgaris	A species of gram-negative, anaerobic, rod-shaped bacteria isolated from soil, animal intestines and feces, and fresh and salt water.