Formylmethanofuran: tetrahydromethanopterin formyltransferase and N 5,N 10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea
| Autor: | J. Breitung, Karl-Otto Stetter, Rudolf K. Thauer, Beatrix Schwörer, Andreas R. Klein |
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| Rok vydání: | 1993 |
| Předmět: |
Hydroxymethyl and Formyl Transferases
animal structures Molecular Sequence Data Dehydrogenase Euryarchaeota Methanofuran Biochemistry Microbiology chemistry.chemical_compound Species Specificity Transferases Enzyme Stability Genetics Amino Acid Sequence Molecular Biology chemistry.chemical_classification Oxidoreductases Acting on CH-NH Group Donors biology Archaeoglobus fulgidus Tetrahydromethanopterin General Medicine Hydrogen-Ion Concentration biology.organism_classification Archaea Coenzyme F420 Molecular Weight Kinetics Enzyme chemistry Methylenetetrahydromethanopterin dehydrogenase |
| Zdroj: | Archives of Microbiology. 159:225-232 |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/bf00248476 |
| Popis: | The sulfate-reducing Archaeoglobus fulgidus contains a number of enzymes previously thought to be unique for methanogenic Archaea. The purification and properties of two of these enzymes, of formylmethanofuran: tetrahydromethanopterin formyltransferase and of N5,N10-methylenetetrahydromethanopterin dehydrogenase (coenzyme F420 dependent) are described here. A comparison of the N-terminal amino acid sequences and of other molecular properties with those of the respective enzymes from three methanogenic Archaea revealed a high degree of similarity. |
| Databáze: | OpenAIRE |
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