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Engineering a non-model yeast Rhodotorula mucilaginosa for terpenoids synthesis

Synthetic and Systems Biotechnology 2024年第3期9卷 569-576页

作者： Qiongqiong Chen Liting Lyu haizhao xue Aabid Manzoor Shah Zongbao Kent Zhao Laboratory of Biotechnology Dalian Institute of Chemical PhysicsCAS457 Zhongshan RoadDalian116023China MOE Key Laboratory of Bio-Intelligent Manufacturing School of BioengineeringDalian University of TechnologyDalian116024China University of Chinese Academy of Sciences 19 Yuquan RoadBeijing100049China

Terpenoids have tremendous biological activities and are widely employed in food,healthcare and pharmaceutical *** synthetic biology to product terpenoids from microbial cell factories presents a promising alternative route compared to conventional methods such as chemical synthesis or *** red yeast Rhodotorula mucilaginosa has been widely studied due to its natural production capacity of carotenoid and lipids,indicating a strong endogenous isoprene pathway with readily available metabolic *** study constructed several engineered strains of *** with the aim of producing different ***α-terpineol was produced by expressing theα-terpineol synthase from Vitis *** titer ofα-terpineol was further enhanced to 0.39 mg/L by overexpressing the endogenous rate-limiting gene of the MVA *** ofα-farnesene synthase from Malus domestica,in combination with MVA pathway rate-limiting gene resulted in significant increase inα-farnesene production,reaching a titer of 822 mg/*** carotenoid degradation productβ-ionone was produced at a titer of 0.87 mg/L by expressing theβ-ionone synthase from Petunia *** study demonstrates the potential of *** as a platform host for the direct biosynthesis of various terpenoids and provides insights for further development of such platforms.

关键词： Rhodotorula mucilaginosa Synthetic biology α-Terpineol β-Ionone α-Farnesene

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Creation of cytochrome P450 catalysis depending on a non-natural cofactor for fatty acid hydroxylation

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Journal of Energy Chemistry 2023年第4期79卷 31-36页

作者： Qing Li Xiaojia Guo xueying Wang Junting Wang Li Wan haizhao xue Zongbao K.Zhao Laboratory of Biotechnology Dalian Institute of Chemical PhysicsChinese Academy of SciencesDalian 116023LiaoningChina University of Chinese Academy of Sciences Beijing 100049China State Key Laboratory of Catalysis Dalian Institute of Chemical PhysicsChinese Academy of SciencesDalian 116023LiaoningChina Dalian Key Laboratory of Energy Biotechnology Dalian Institute of Chemical PhysicsChinese Academy of SciencesDalian 116023LiaoningChina

Cytochrome P450 enzymes catalyze diverse oxidative transformations at the expense of reduced nicotinamide adenine dinucleotide phosphate(NADPH),however,their applications remain limited largely because NADPH is cost-prohibitive for biocatalysis at scale yet tightly regulated in host cells.A highly challenging task for P450 catalysis has been to develop an alternative and biocompatible electrondonating *** we engineered P450 BM3 to favor reduced nicotinamide cytosine dinucleotide(NCDH)and created non-natural cofactor-dependent P450 *** outstanding mutants were identified with over 640-fold NCDH preference improvement and good catalytic efficiencies of over15,000 M^(-1)s^(-1)for the oxidation of the fatty acid probe 12-(para-nitrophenoxy)-*** docking analysis indicated that these mutants bear a compacted cofactor *** fusing with an NCD-dependent formate dehydrogenase,fused proteins functioned as NCDH-specific P450catalysts by using formate as the electron ***,these mutants and fusions catalyzed NCDH-dependent hydroxylation of fatty acids with similar chain length preference to those by natural P450 BM3 in the presence of NADPH and also similar regioselectivity for subterminal hydroxylation of lauric *** P450 BM3 and its variants are catalytically powerful to take diverse substrates and convey different reaction paths,our results offer an exciting opportunity to devise advanced cell factories that convey oxidative biocatalysis with an orthogonal reducing power supply system.

关键词： Biocatalysis Cytochrome P450 Directed evolution Fatty acid hydroxylation Non-natural cofactor Synthetic biology

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基于理性设计提高1,3-丙二醇氧化还原酶的稳定性和活性

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食品与发酵工业 2023年第16期49卷 18-25页

作者：付凯璇王雪颖黄彦喆薛海曌胡英菡赵宗保中国科学院大连化学物理研究所辽宁大连116000 中国科学院大学北京100000

1,3-丙二醇氧化还原酶(1,3-propanediol oxidoreductase,PDOR)是甘油生物合成1,3-丙二醇(1,3-propanediol,1,3-PD)的关键限速酶之一。使用PoPMuSiC 2.1计算肺炎克雷伯菌(Klebsiella pneumoniae)来源PDOR(KpPDOR)突变的折叠自由能,结合HotSpot Wizard 3.0对催化中心附近氨基酸的功能热点分析和保守残基鉴定,理性选取突变位点,构建定点突变。经诱导表达、蛋白纯化和酶学性质研究,获得催化性能、热稳定性和pH耐受性提高的突变体。V155N突变体在37℃,pH 7.5下的还原活性为KpPDOR的1.7倍,pH 4.0时是KpPDOR的2.5倍。N262E突变体37℃下半衰期为KpPDOR的1.4倍。分析蛋白结构,发现Val155突变为Asn导致新形成两个氢键,稳定了Val155所在的β-折叠结构。而Asn262突变为Glu形所成的两个氢键,可增强催化中心刚性,提升酶稳定性。静息细胞转化甘油合成1,3-PD,发现突变体V155N工程菌株1,3-PD产能为1.16 mmol/L/OD_(600),高于野生型KpPDOR工程菌株的0.82 mmol/L/OD_(600)。此理性设计方法对改良其他工业酶的性能有一定参考价值。

关键词： 1,3-丙二醇 1,3-丙二醇氧化还原酶理性设计热稳定性 pH耐受性

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