Rius N, Maeda K, Demain A L
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139-4307, USA.
FEMS Microbiol Lett. 1996 Nov 1;144(2-3):207-11. doi: 10.1111/j.1574-6968.1996.tb08532.x.
L-Lysine epsilon-aminotransferase (LAT) catalyzes the first reaction in the two-step conversion of L-lysine (Lys) to 1-alpha-aminoadipic acid (Aaa), a direct precursor of cephalosporins (including cephamycin C) in Streptomyces clavuligerus. Previous work showed that addition of Lys to chemically defined medium improved antibiotic production. We show that in S. clavuligerus cultures supplemented with high concentrations of Lys, Lys enhances antibiotic production by a dual effect, i.e. as a substrate of LAT thus providing Aaa and also as an inducer of LAT yielding even more Aaa. On the other hand, LAT is not induced by Aaa.
L-赖氨酸ε-氨基转移酶(LAT)催化L-赖氨酸(Lys)两步转化为1-α-氨基己二酸(Aaa)的第一步反应,1-α-氨基己二酸是棒状链霉菌中头孢菌素(包括头霉素C)的直接前体。先前的研究表明,在化学成分确定的培养基中添加赖氨酸可提高抗生素产量。我们发现,在添加高浓度赖氨酸的棒状链霉菌培养物中,赖氨酸通过双重作用提高抗生素产量,即作为LAT的底物从而提供Aaa,同时作为LAT的诱导剂产生更多的Aaa。另一方面,Aaa不会诱导LAT。