NAD+激酶
化学
乳糖
立体化学
ATP合酶
环烯醚萜
背景(考古学)
氧化还原酶
氢化物
基质(水族馆)
酶
氢
生物化学
有机化学
内酯
生物
古生物学
生态学
糖苷
作者
Yumei Hu,Weidong Liu,Satish R. Malwal,Yingying Zheng,Xinxin Feng,Tzu‐Ping Ko,Chun‐Chi Chen,Zixiang Xu,Meixia Liu,Xu Han,Jian Gao,Eric Oldfield,Rey‐Ting Guo
标识
DOI:10.1002/ange.201508310
摘要
Abstract Structures of the iridoid synthase nepetalactol synthase in the presence of NAD + , NADPH or NAD + /10‐oxogeranial were solved. The 10‐oxogeranial substrate binds in a transoid ‐O1‐C3 conformation and can be reduced by hydride addition to form the byproduct S ‐10‐oxo‐citronellal. Tyr178 Oζ is positioned 2.5 Å from the substrate O1 and provides the second proton required for reaction. Nepetalactol product formation requires rotation about C1–C2 to form the cisoid isomer, leading to formation of the cis ‐enolate, together with rotation about C4–C5, which enables cyclization and lactol production. The structure is similar to that of progesterone‐5β‐reductase, with almost identical positioning of NADP, Lys146(147), Tyr178(179), and F342(343), but only Tyr178 and Phe342 appear to be essential for activity. The transoid 10‐oxogeranial structure also serves as a model for β‐face hydride attack in progesterone 5β‐reductases and is of general interest in the context of asymmetric synthesis.
科研通智能强力驱动
Strongly Powered by AbleSci AI