Schmidt H, Bode R
Institut für Biochemie, Fachrichtung Biologie, Ernst-Moritz-Arndt-Universität Greifswald, Germany.
Antonie Van Leeuwenhoek. 1992 Nov;62(4):285-90. doi: 10.1007/BF00572596.
A novel aminotransferase catalyzing the second step of lysine catabolism, the oxidative transamination of the alpha-group of N6-acetyllysine, was identified and characterized in the yeast Candida 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 microM for pyridoxal-5-phosphate. The enzyme had a maximum activity at pH 8.1 and 32 degrees 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.
在麦芽糖假丝酵母中鉴定并表征了一种新型转氨酶，该酶催化赖氨酸分解代谢的第二步，即N6 - 乙酰赖氨酸α-基团的氧化转氨作用。该酶在以L-赖氨酸作为唯一碳源生长的细胞中被强烈诱导。其活性对N6 - 乙酰赖氨酸和2-氧代戊二酸均具有特异性。供体的Km值为14 mM，受体的Km值为4 mM，磷酸吡哆醛的Km值为1.7 μM。该酶在pH 8.1和32℃时具有最大活性。通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳估计其分子量为55 kDa。由于通过凝胶过滤测定的天然分子量为120 kDa，该酶可能是同型二聚体。
