Abstract
A novel aminotransferase catalyzing the second step of lysine catabolism, the oxidative transamination of the α-group of N6-acetyllysine, was identified and characterized in the yeastCandida maltosa. The enzyme was strongly induced in cells grown on L-lysine as sole carbon source. Its activity was specific for both N6-acetyllysine and 2-oxoglutarate. The Km values were 14 mM for the donor, 4 mM for the acceptor and 1.7 μM for pyridoxal-5-phosphate. The enzyme had a maximum activity at pH 8.1 and 32°C. Its molecular mass estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis was 55 kDa. Since the native molecular mass determined by gel filtration was 120 kDa, the enzyme is probably a homodimer.
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Schmidt, H., Bode, R. Characterization of a novel enzyme, N6-acetyl-L-lysine: 2-oxoglutarate aminotransferase, which catalyses the second step of lysine catabolism inCandida maltosa . Antonie van Leeuwenhoek 62, 285–290 (1992). https://doi.org/10.1007/BF00572596
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DOI: https://doi.org/10.1007/BF00572596