Purification and N-terminal amino-acid sequences of bacterial malate dehydrogenases from six actinomycetales strains and from Phenylobacterium immobile, strain E.
Malate dehydrogenases from Streptosporangium roseum (DSM 43021), Planomonospora venezuelensis (DSM 43178), Microtetraspora glauca (ATCC 23057), Actinoplanes missouriensis (DSM 43046), Streptomyces atratus (ATCC 14046), Kibdelosporangium aridum (ATCC 39323), and from Phenylobacterium immobile, strain E (DSM 1986) were purified to homogeneity. The N-terminal amino-acid sequences were determined and compared with known prokaryotic and eukaryotic sequence data. The partial sequences from Actinomycetales enzymes include a string of amino acids which is also present in the N-terminal region of malate dehydrogenases from Thermus flavus and from mammalian cytoplasm.
Institut für Mikrobiologie, Universität Hohenheim.
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Rommel
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Hund
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Speth
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Lingens
D000192:Actinomycetales / Q000201:enzymology*; D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D008291:Malate Dehydrogenase / Q000032:analysis* / Q000302:isolation & purification; D008969:Molecular Sequence Data
D003470:Culture Media; D008291:Malate Dehydrogenase; D000645:Ammonium Sulfate