干旱区生态环境知识资源中心(Arid): Two new ene-reductases from photosynthetic extremophiles enlarge the panel of old yellow enzymes: CtOYE and GsOYE

Arid

DOI	10.1007/s00253-019-10287-2
	Two new ene-reductases from photosynthetic extremophiles enlarge the panel of old yellow enzymes: CtOYE and GsOYE
	Robescu, Marina Simona 1; Niero, Mattia 1; Hall, Melanie 2; Cendron, Laura 1; Bergantino, Elisabetta 1
通讯作者	Cendron, Laura ; Bergantino, Elisabetta
来源期刊	APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
ISSN	0175-7598
EISSN	1432-0614
出版年	2020
卷号	104 期号:5 页码:2051-2066
英文摘要	Looking for new ene-reductases with uncovered features beneficial for biotechnological applications, by mining genomes of photosynthetic extremophile organisms, we identified two new Old Yellow Enzyme homologues: CtOYE, deriving from the cyanobacterium Chroococcidiopsis thermalis, and GsOYE, from the alga Galdieria sulphuraria. Both enzymes were produced and purified with very good yields and displayed catalytic activity on a broad substrate spectrum by reducing alpha,beta-unsaturated ketones, aldehydes, maleimides and nitroalkenes with good to excellent stereoselectivity. Both enzymes prefer NADPH but demonstrate a good acceptance of NADH as cofactor. CtOYE and GsOYE represent robust biocatalysts showing high thermostability, a wide range of pH optimum and good co-solvent tolerance. High resolution X-ray crystal structures of both enzymes have been determined, revealing conserved features of the classical OYE subfamily as well as unique properties, such as a very long loop entering the active site or an additional C-terminal alpha helix in GsOYE. Not surprisingly, the active site of CtOYE and GsOYE structures revealed high affinity toward anions caught from the mother liquor and trapped in the anion hole where electron-withdrawing groups such as carbonyl group are engaged. Ligands (para-hydroxybenzaldehyde and 2-methyl-cyclopenten-1-one) added on purpose to study complexes of GsOYE were detected in the enzyme catalytic cavity, stacking on top of the FMN cofactor, and support the key role of conserved residues and FMN cofactor in the catalysis.
英文关键词	Biocatalysis Ene-reductases Extremophiles OYE
类型	Article
语种	英语
国家	Italy ; Austria
收录类别	SCI-E
WOS记录号	WOS:000529946400019
WOS关键词	ACTIVATED C=C-BONDS ; X-RAY-STRUCTURE ; ASYMMETRIC BIOREDUCTION ; STRUCTURAL INSIGHT ; SPECIFICITY ; REDUCTION ; DISCOVERY ; FAMILY ; EXPRESSION ; DESERT
WOS类目	Biotechnology & Applied Microbiology
WOS研究方向	Biotechnology & Applied Microbiology
资源类型	期刊论文
条目标识符	http://119.78.100.177/qdio/handle/2XILL650/318509
作者单位	1.Univ Padua, Dept Biol, Viale G Colombo 3, Padua 35131, Italy; 2.Karl Franzens Univ Graz, Dept Chem, Heinrichstr 28, Graz 8010, Austria
推荐引用方式 GB/T 7714	Robescu, Marina Simona,Niero, Mattia,Hall, Melanie,et al. Two new ene-reductases from photosynthetic extremophiles enlarge the panel of old yellow enzymes: CtOYE and GsOYE[J],2020,104(5):2051-2066.
APA	Robescu, Marina Simona,Niero, Mattia,Hall, Melanie,Cendron, Laura,&Bergantino, Elisabetta.(2020).Two new ene-reductases from photosynthetic extremophiles enlarge the panel of old yellow enzymes: CtOYE and GsOYE.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,104(5),2051-2066.
MLA	Robescu, Marina Simona,et al."Two new ene-reductases from photosynthetic extremophiles enlarge the panel of old yellow enzymes: CtOYE and GsOYE".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 104.5(2020):2051-2066.