Fellows F C
Biochem J. 1973 Oct;136(2):321-7. doi: 10.1042/bj1360321.
Lysine-2-oxoglutarate reductase was prepared from ox liver and its characteristics were examined. Its activity was totally inhibited in the presence of NH(4)Cl. Under conditions that inhibit saccharopine formation, and in the presence of NADP(+), ox liver mitochondria were found to catalyse the hydrolysis of saccharopine to lysine and alpha-oxoglutarate. The enzyme involved was named saccharopine oxidoreductase. It was partially purified and separated from lysine-oxoglutarate reductase. Comparison of the properties of these two enzymes showed that saccharopine degradation was stimulated under conditions that inhibit its formation. The effect of pH, various cofactors and stability during incubation confirm that saccharopine biosynthesis from, and degradation to, lysine are catalysed by two distinct enzymes.
从牛肝脏中制备了赖氨酸-2-氧代戊二酸还原酶,并对其特性进行了研究。在氯化铵存在的情况下,其活性被完全抑制。在抑制酵母氨酸形成的条件下,且存在烟酰胺腺嘌呤二核苷酸磷酸(NADP⁺)时,发现牛肝脏线粒体可催化酵母氨酸水解为赖氨酸和α-氧代戊二酸。所涉及的酶被命名为酵母氨酸氧化还原酶。它被部分纯化并与赖氨酸-氧代戊二酸还原酶分离。对这两种酶的特性比较表明,在抑制酵母氨酸形成的条件下,其降解受到刺激。pH值、各种辅因子以及孵育过程中的稳定性的影响证实,赖氨酸的酵母氨酸生物合成和降解是由两种不同的酶催化的。