Lee H J, Monder C
Biochemistry. 1977 Aug 23;16(17):3810-4. doi: 10.1021/bi00636a014.
Enzyme activity which catalyzes the oxidation of 11-deoxycorticosterone to 21-oic acids accompanies the "detritiating" enzyme (isomerase) of hamster liver recently isolated by Martin, K. O., et al. ((1977) Biochemistry 16 (preceding paper in this issue)). The metabolites isolated were 20alpha- and 20beta-hydroxy-3-oxo-pregn-4-en-21-oic acid and 3,20-dioxo-pregn-4-en-21-oic acid. When 21-hydroxy[4-14C, 21-3H]pregn-4-en-3,20-dione was the substrate, about half of the tritium was retained in position 20 of the hydroxy acids. The system which catalyzes the conversion of the ketol side chain of corticosteroids to acid metabolites appears to be a cluster of closely related enzymes. As a result of these studies, we believe that the hamster liver enzyme preparation provides a useful model system for studies on the biosynthesis of acid metabolites of the corticosteroids in man.
催化11-脱氧皮质酮氧化为21-酸的酶活性与马丁等人((1977)《生物化学》16卷(本期前一篇论文))最近分离出的仓鼠肝脏“脱氚”酶(异构酶)相伴。分离出的代谢产物为20α-和20β-羟基-3-氧代-孕-4-烯-21-酸以及3,20-二氧代-孕-4-烯-21-酸。当21-羟基[4-¹⁴C, 21-³H]孕-4-烯-3,20-二酮作为底物时,约一半的氚保留在羟基酸的20位。催化皮质类固醇酮醇侧链转化为酸性代谢产物的系统似乎是一组密切相关的酶。这些研究的结果使我们相信,仓鼠肝脏酶制剂为研究人类皮质类固醇酸性代谢产物的生物合成提供了一个有用的模型系统。