Chun‐Chi Chen

ORCID: 0000-0002-7459-5591
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Research Areas
  • Microbial Natural Products and Biosynthesis
  • Plant biochemistry and biosynthesis
  • Enzyme Production and Characterization
  • Biofuel production and bioconversion
  • Enzyme Structure and Function
  • Enzyme Catalysis and Immobilization
  • biodegradable polymer synthesis and properties
  • Natural product bioactivities and synthesis
  • Microplastics and Plastic Pollution
  • Microbial Metabolites in Food Biotechnology
  • Metal-Catalyzed Oxygenation Mechanisms
  • Microbial Metabolic Engineering and Bioproduction
  • Biochemical and Molecular Research
  • Pharmacogenetics and Drug Metabolism
  • Mycotoxins in Agriculture and Food
  • RNA and protein synthesis mechanisms
  • Carbohydrate Chemistry and Synthesis
  • Advanced biosensing and bioanalysis techniques
  • Genomics and Phylogenetic Studies
  • Computational Drug Discovery Methods
  • Hepatitis B Virus Studies
  • Microbial bioremediation and biosurfactants
  • Recycling and Waste Management Techniques
  • Photosynthetic Processes and Mechanisms
  • Effects and risks of endocrine disrupting chemicals

Hangzhou Normal University
2023-2025

Hubei University
2018-2025

Chinese Academy of Sciences
2012-2025

Tianjin Institute of Industrial Biotechnology
2013-2025

National Kaohsiung First University of Science and Technology
2025

National Kaohsiung University of Science and Technology
2025

National Chiayi University
2023-2024

Xiamen University of Technology
2022-2023

Longyan University
2021-2022

National Yang Ming Chiao Tung University
2007-2020

Abstract PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present structures a novel PETase from PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, activity measurements, substrate-binding mode is proposed, several features critical catalysis are elucidated.

10.1038/s41467-017-02255-z article EN cc-by Nature Communications 2017-12-07

Abstract Poly(butylene adipate-co-terephthalate) (PBAT), a polyester made of terephthalic acid (TPA), 1,4-butanediol, and adipic acid, is extensively utilized in plastic production has accumulated globally as environmental waste. Biodegradation an attractive strategy to manage PBAT, but effective PBAT-degrading enzyme required. Here, we demonstrate that cutinases are highly potent enzymes can completely decompose PBAT films 48 h. We further show the engineered cutinases, by applying double...

10.1038/s41467-023-37374-3 article EN cc-by Nature Communications 2023-03-24

KRAS mutation occurs in nearly 30% of human cancers, yet the most prevalent and oncogenic KRAS(G12D) variant still lacks inhibitors. Herein, we designed a series potent inhibitors that can form salt bridge with KRAS's Asp12 residue. Our ITC results show these have similar binding affinity both GDP-bound GTP-bound KRAS(G12D), our crystallographic studies reveal structural basis inhibitor binding-induced switch-II pocket experimentally confirming formation between piperazine moiety residue...

10.1038/s41421-021-00368-w article EN cc-by Cell Discovery 2022-01-25

Polyethylene terephthalate (PET) is among the most extensively produced plastics, but huge amounts of PET wastes that have accumulated in environment become a serious threat to ecosystem. Applying hydrolytic enzymes depolymerize an attractive measure manage pollution, and searching for more effective prerequisite achieve this goal. A thermostable cutinase originates from leaf-branch compost termed ICCG hydrolase reported so far. Here, we illustrated crystal structure complex with analogue,...

10.1021/acscatal.1c05800 article EN ACS Catalysis 2022-02-18

In both cancer and infections, diseased cells are presented to human Vγ9Vδ2 T through an 'inside out' signalling process whereby structurally diverse phosphoantigen (pAg) molecules sensed by the intracellular domain of butyrophilin BTN3A11-4. Here we show how-in humans alpaca-multiple pAgs function as 'molecular glues' promote heteromeric association between domains BTN3A1 similar BTN2A1. X-ray crystallography studies visualized that engagement with forms a composite interface for direct...

10.1038/s41586-023-06525-3 article EN cc-by Nature 2023-09-06

Cancer stem cell (CSC) theory has drawn much attention, with evidence supporting the contribution of cells to tumor initiation, relapse, and therapy resistance.To screen drugs that target CSCs improve current treatment outcome overcome drug resistance in patients lung cancer.We used publicly available embryonic CSC-associated gene signatures query Connectivity Map for potential can, at least part, reverse expression profile CSCs. High scores were noted several phenothiazine-like...

10.1164/rccm.201207-1180oc article EN American Journal of Respiratory and Critical Care Medicine 2012-10-01

The lack of a suitable in vitro hepatitis B virus (HBV) infectivity model has limited examination the early stages virus-cell interaction. In this study, we used an immortalized cell line derived from human primary hepatocytes, HuS-E/2, to study mechanism HBV infection. infection efficiency was markedly increased after dimethyl sulfoxide (DMSO)-induced differentiation cells. Transmission electron microscopy demonstrated presence intact particles DMSO-treated HBV-infected HuS-E/2 cells, which...

10.1128/jvi.00873-12 article EN Journal of Virology 2012-06-28

Many steroids are important pharmaceutically active compounds, while cytochrome P450 monooxygenases (CYPs) attractive enzymes for applications in steroidal drug synthesis. However, the catalytic efficiency of existing P450s is not routinely high enough, as well molecular basis selectivity control unclear, which severely restrict their real applications. Here, a 16β steroid-hydroxylase CYP109B4 from Bacillus sonorensis identified with excellent and activity. The crystallization structural...

10.1021/acscatal.2c04906 article EN ACS Catalysis 2023-01-06

The catalytic domain of XynCDBFV, a glycoside hydrolase family 11 (GH11) xylanase from ruminal fungus Neocallimastix patriciarum previously engineered to exhibit higher specific activity and broader pH adaptability, holds great potential in commercial applications. Here, the crystal structures XynCDBFV its complex with substrate were determined 1.27–1.43 Å resolution. These revealed typical GH11 β-jelly-roll fold detailed interaction networks between enzyme ligands. Notably, an extended...

10.1074/jbc.m114.550905 article EN cc-by Journal of Biological Chemistry 2014-03-12

Trypanosomatid parasites are the causative agents of many neglected tropical diseases and there is currently considerable interest in targeting endogenous sterol biosynthesis these organisms as a route to development novel anti-infective drugs. Here, we report first x-ray crystallographic structures enzyme squalene synthase (SQS) from trypanosomatid parasite, Trypanosoma cruzi, agent Chagas disease. We obtained five T. cruzi SQS eight human with four classes inhibitors: substrate-analog...

10.1371/journal.ppat.1004114 article EN cc-by PLoS Pathogens 2014-05-01

Abstract Cytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions. Self-sufficient cytochrome contain the redox partners in single polypeptide chain. Here, we present crystal structure full-length CYP116B46, self-sufficient P450. The continuous chain comprises three functional domains, which align well with direction electrons traveling from FMN to heme through [2Fe-2S] cluster. and cluster positioned closely, facilitates efficient electron...

10.1038/s41467-020-16500-5 article EN cc-by Nature Communications 2020-05-29

Imine reductases (IREDs) are increasingly identified and characterized for the reduction of imines reductive amination ketones. However, their practical application is still limited due to low activity poor stability native enzymes. Herein, we developed an engineered IRED through three rounds evolution from wild-type Streptomyces clavuligerus. The specific enzyme, ScIRED-R3-V4, was increased >100-fold, >270-fold. Using more active stable 80 g L–1 cyclic imine 2-(2,5-difluorophenyl)-pyrroline...

10.1021/acscatal.2c03783 article EN ACS Catalysis 2022-11-21

As the RNA secondary structure is highly related to its stability and functions, prediction of great value biological research. The traditional computational for mainly based on thermodynamic model with dynamic programming find optimal structure. However, performance approach unsatisfactory further Besides, complexity using [Formula: see text]; it becomes text] pseudoknots, which computationally impractical large-scale analysis.In this paper, we propose REDfold, a novel deep learning-based...

10.1186/s12859-023-05238-8 article EN cc-by BMC Bioinformatics 2023-03-28

Pullulanase is a debranching enzyme that specifically hydrolyzes the α-1,6 glycosidic linkage of α-glucans, and has wide industrial applications. Here, we report structural functional studies new thermostable pullulanase from Anoxybacillus sp. LM18-11 (PulA). Based on hydrolysis products, PulA was classified as type I pullulanase. It showed maximum activity at 60°C pH 6.0. Kinetic study specific Km for pullulan are 750 U mg−1 16.4 μmol L−1, respectively. half-life 48 h 60°C. The remarkable...

10.1002/prot.24498 article EN Proteins Structure Function and Bioinformatics 2013-12-17

We report the results of an investigation activity a series amidine and bisamidine compounds against Staphylococcus aureus Escherichia coli. The most active bound to AT-rich DNA dodecamer (CGCGAATTCGCG)2 using DSC were found increase melting transition by up 24 °C. Several also inhibited undecaprenyl diphosphate synthase (UPPS) with IC50 values 100-500 nM, we good correlations (R(2) = 0.89, S. aureus; R(2) 0.79, E. coli) between experimental predicted cell growth inhibition ΔTm UPPS together...

10.1021/jm501449u article EN Journal of Medicinal Chemistry 2015-01-09
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