Shengying Li

Prof. Dr. Shengying Li

orcid

Research Focus & Metrics

Academic Career Length

14Years (2013-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
4 September 2024 in Nature
Verified
Journal Article
Open access
PDF file
JCJianwei Chen
Jianwei Chen
YJYangyang Jia
Yangyang Jia
YSYing Sun
Ying Sun
KLKun Liu
Kun Liu
CZChanghao Zhou
Changhao Zhou
GFGuangyi Fan
Guangyi Fan
The past two decades has witnessed a remarkable increase in the number of microbial genomes retrieved from marine systems1,2. However, it has remained challenging to translate this marine genomic diversity into biotechnological and biomedical applications3,4. Here we recovered 43,191 bacterial and archaeal genomes from publicly available marine metagenomes, encompassing a wide range of diversity with 138 distinct phyla, redefining the upper limit of marine bacterial genome size and revealing complex trade-offs between the occurrence of CRISPR–Cas systems and antibiotic resistance genes. In silico bioprospecting of these marine genomes led to the discovery of a novel CRISPR–Cas9 system, ten antimicrobial peptides, and three enzymes that degrade polyethylene terephthalate. In vitro experiments confirmed their effectiveness and efficacy. This work provides evidence that global-scale sequencing initiatives advance our understanding of how microbial diversity has evolved in the oceans and is maintained, and demonstrates how such initiatives can be sustainably exploited to advance biotechnology and biomedicine.

3 August 2017 in Natural Product Reports
Verified
Journal Article
Closed access
PDF file
XXingwang Zhang
Xingwang Zhang
SLShengying Li
Shengying Li
Covering: 2000 to 2017 Cytochrome P450 enzymes (P450s) are the most versatile biocatalysts in nature. The catalytic competence of these extraordinary hemoproteins is broadly harnessed by numerous chemical defenders such as bacteria, fungi, and plants for the generation of diverse and complex natural products. Rather than the common tailoring reactions (e.g. hydroxylation and epoxidation) mediated by the majority of biosynthetic P450s, in this review, we will focus on the unusual P450 enzymes in relation to new chemistry, skeleton construction, and structure re-shaping via their own unique catalytic power or the intriguing protein–protein interactions between P450s and other proteins. These uncommon P450 reactions lead to a higher level of chemical space expansion for natural products, through which a broader spectrum of bioactivities can be gained by the host organisms.

12 March 2021 in Natural Product Reports
Verified
Journal Article
Closed access
PDF file
XXingwang Zhang
Xingwang Zhang
JGJiawei Guo
Jiawei Guo
FCFangyuan Cheng
Fangyuan Cheng
SLShengying Li
Shengying Li
P450s play crucial roles in fungal natural product biosynthesis by mediating various common and uncommon reactions.

1 June 2020 in Trends in Microbiology
Verified
Journal Article
Closed access
SLShengying Li
Shengying Li
LDLei Du
Lei Du
RBRita Bernhardt
Rita Bernhardt

1 January 2014 in Biotechnology for Biofuels
Verified
Journal Article
Open access
PDF file
YLYi Liu
Yi Liu
CWCong Wang
Cong Wang
JYJinyong Yan
Jinyong Yan
WZWei Zhang
Wei Zhang
WGWenna Guan
Wenna Guan
SLShengying Li
Shengying Li
Cytochrome P450 OleTJE from Jeotgalicoccus sp. ATCC 8456, a new member of the CYP152 peroxygenase family, was recently found to catalyze the unusual decarboxylation of long-chain fatty acids to form α-alkenes using H2O2 as the sole electron and oxygen donor. Because aliphatic α-alkenes are important chemicals that can be used as biofuels to replace fossil fuels, or for making lubricants, polymers and detergents, studies on OleTJE fatty acid decarboxylase are significant and may lead to commercial production of biogenic α-alkenes in the future, which are renewable and more environmentally friendly than petroleum-derived equivalents.

28 September 2018 in ACS Catalysis
Verified
Journal Article
Closed access
WZWei Zhang
Wei Zhang
LDLei Du
Lei Du
FLFengwei Li
Fengwei Li
XZXingwang Zhang
Xingwang Zhang
ZQZepeng Qu
Zepeng Qu
SLShengying Li
Shengying Li