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The Promiscuity of Squalene Synthase-Like Enzyme: Dehydrosqualene Synthase, a Natural Squalene Hyperproducer?

التفاصيل البيبلوغرافية
العنوان: The Promiscuity of Squalene Synthase-Like Enzyme: Dehydrosqualene Synthase, a Natural Squalene Hyperproducer?
المؤلفون: Guan Z; Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands., Song Y; Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands.; Guangdong Provincial Key Laboratory of Microbial Culture Collection and Application, State Key Laboratory of Applied Microbiology Southern China, Institute of Microbiology, Guangdong Academy of Sciences, Guangzhou510070, China., de Vries M; Interfaculty Mass Spectrometry Center, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands., Permentier H; Interfaculty Mass Spectrometry Center, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands., Tepper P; Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands., van Merkerk R; Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands., Setroikromo R; Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands., Quax WJ; Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen9713 AV, The Netherlands.
المصدر: Journal of agricultural and food chemistry [J Agric Food Chem] 2024 Feb 14; Vol. 72 (6), pp. 3017-3024. Date of Electronic Publication: 2024 Feb 05.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0374755 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5118 (Electronic) Linking ISSN: 00218561 NLM ISO Abbreviation: J Agric Food Chem Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, American Chemical Society.
مواضيع طبية MeSH: Squalene*/*analogs & derivatives, Squalene*/metabolism , Farnesyl-Diphosphate Farnesyltransferase*/genetics , Farnesyl-Diphosphate Farnesyltransferase*/metabolism, Tandem Mass Spectrometry ; Terpenes/metabolism ; Nitric Oxide Synthase
مستخلص: Dehydrosqualene synthase (CrtM), as a squalene synthase-like enzyme from Staphylococcus aureus , can naturally utilize farnesyl diphosphate to produce dehydrosqualene (C 30 H 48 ). However, no study has documented the natural production of squalene (C 30 H 50 ) 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 (C 40 H 64 ). 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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فهرسة مساهمة: Keywords: CrtM; SQS; enzyme promiscuity; squalene; terpenoid
المشرفين على المادة: 11051-27-7 (dehydrosqualene)
7QWM220FJH (Squalene)
EC 2.5.1.21 (Farnesyl-Diphosphate Farnesyltransferase)
0 (Terpenes)
EC 1.14.13.39 (Nitric Oxide Synthase)
تواريخ الأحداث: Date Created: 20240205 Date Completed: 20240215 Latest Revision: 20240218
رمز التحديث: 20240218
مُعرف محوري في PubMed: PMC10870770
DOI: 10.1021/acs.jafc.3c05770
PMID: 38315649
قاعدة البيانات: MEDLINE
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