角鲨烯
ATP合酶
酶
化学
法尼基二磷酸法尼基转移酶
生物化学
法尼酰转移酶
预酸化
作者
Guoqiang Zheng,Yafeng Song,Marcel de Vries,Hjalmar P. Permentier,Pieter G. Tepper,Ronald van Merkerk,Rita Setroikromo,Wim J. Quax
标识
DOI:10.1021/acs.jafc.3c05770
摘要
Dehydrosqualene synthase (CrtM), as a squalene synthase-like enzyme from Staphylococcus aureus, can naturally utilize farnesyl diphosphate to produce dehydrosqualene (C30H48). However, no study has documented the natural production of squalene (C30H50) by CrtM. Here, based on an HPLC-Q-Orbitrap-MS/MS study, we report that the expression of crtM in vitro or in Bacillus subtilis 168 both results in the output of squalene, dehydrosqualene, and phytoene (C40H64). Notably, wild-type CrtM exhibits a significantly higher squalene yield compared to squalene synthase (SQS) from Bacillus megaterium with an approximately 2.4-fold increase. Moreover, the examination of presqualene diphosphate’s stereostructures in both CrtM and SQS enzymes provides further understanding into the presence of multiple identified terpenoids. In summary, this study not only provides insights into the promiscuity demonstrated by squalene synthase-like enzymes but also highlights a new strategy of utilizing CrtM as a potential replacement for SQS in cell factories, thereby enhancing squalene production.
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