A biochemical and immunological study has revealed a new formate dehydrogenase isoenzyme in Escherichia coli. The enzyme is an isoenzyme of the respiratory formate dehydrogenase (FDH-N) which forms part of the formate to nitrate respiratory pathway found in the organisms when it is grown anaerobically in the presence of nitrate. The new enzyme, termed FDH-Z, cross reacts with antibodies raised to FDH-N and possesses a similar polypeptide composition to FDH-N. FDH-Z catalyses the phenazine methosulphate-linked formate dehydrogenase activity present in the aerobically-grown bacterium. FDH-Z and FDH-N exhibit distinct regulation. Like formate dehydrogenase N, formate dehydrogenase Z is a membrane-bound molybdoenzyme. With nitrate reductase it can catalyse electron transfer between formate and nitrate. Quinones are required for the physiological electron transfer to nitrate. It seems likely that like FDH-N, FDH-Z functions physiologically as a formate: quinone oxidoreductase.
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http://purl.uniprot.org/cit... | rdfs:comment | A biochemical and immunological study has revealed a new formate dehydrogenase isoenzyme in Escherichia coli. The enzyme is an isoenzyme of the respiratory formate dehydrogenase (FDH-N) which forms part of the formate to nitrate respiratory pathway found in the organisms when it is grown anaerobically in the presence of nitrate. The new enzyme, termed FDH-Z, cross reacts with antibodies raised to FDH-N and possesses a similar polypeptide composition to FDH-N. FDH-Z catalyses the phenazine methosulphate-linked formate dehydrogenase activity present in the aerobically-grown bacterium. FDH-Z and FDH-N exhibit distinct regulation. Like formate dehydrogenase N, formate dehydrogenase Z is a membrane-bound molybdoenzyme. With nitrate reductase it can catalyse electron transfer between formate and nitrate. Quinones are required for the physiological electron transfer to nitrate. It seems likely that like FDH-N, FDH-Z functions physiologically as a formate: quinone oxidoreductase. | lld:uniprot |
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http://purl.uniprot.org/cit... | uniprot:name | Biochim. Biophys. Acta | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Pommier J. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Giordano G. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Mandrand M.A. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Holt S.E. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Boxer D.H. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:date | 1992 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:pages | 305-313 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:title | A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:volume | 1107 | lld:uniprot |
http://purl.uniprot.org/cit... | dc-term:identifier | doi:10.1016/0005-2736(92)90417-K | lld:uniprot |
http://linkedlifedata.com/r... | uniprot:source | http://purl.uniprot.org/cit... | lld:uniprot |
http://linkedlifedata.com/r... | uniprot:source | http://purl.uniprot.org/cit... | lld:uniprot |
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http://linkedlifedata.com/r... | uniprot:source | http://purl.uniprot.org/cit... | lld:uniprot |