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Modulating Enzyme's Conformational Space: Impact of Substrate Binding, Mode Alteration, and Active Site Mutation in DapC, an Aminotransferase Enzyme of Lysine Biosynthetic Pathway.
J Phys Chem B
January 2025
Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
The microbial aminotransferase enzyme DapC is vital for lysine biosynthesis in various Gram-positive bacteria, including . Characterization of the enzyme's conformational dynamics and identifying the key residues for ligand binding are crucial for the development of effective antimicrobials. This study employs atomistic simulations to explore and categorize the dynamics of DapC in comparison to other classes of aminotransferase.
View Article and Find Full Text PDFExploiting the efficient Exo:Cas12i3-5M fusions for robust single and multiplex gene editing in rice.
J Integr Plant Biol
January 2025
State Key Laboratory of Crop Gene Resources and Breeding, Institute of Crop Sciences (ICS), Chinese Academy of Agricultural Sciences (CAAS), Beijing, 100081, China.
The development of a single and multiplex gene editing system is highly desirable for either functional genomics or pyramiding beneficial alleles in crop improvement. CRISPR/Cas12i3, which belongs to the Class II Type V-I Cas system, has attracted extensive attention recently due to its smaller protein size and less restricted canonical "TTN" protospacer adjacent motif (PAM). However, due to its relatively lower editing efficiency, Cas12i3-mediated multiplex gene editing has not yet been documented in plants.
View Article and Find Full Text PDFExpression and purification of recombinant proteins in is a bedrock technique in biochemistry and molecular biology. Expression optimization requires testing different combinations of solubility tags, affinity purification techniques, and site-specific proteases. This optimization is laborious and time consuming as these features are spread across different vector series and require different cloning strategies with varying efficiencies.
View Article and Find Full Text PDFDiscovery of an Enzyme-Activated Fluorogenic Probe for Profiling of Acylaminoacyl-Peptide Hydrolase.
Anal Chem
January 2025
Department of Laboratory Medicine, School of Medicine, Yangtze University, Jingzhou 434023, P.R. China.
Acylaminoacyl-peptide hydrolase (APEH), a serine peptidase that belongs to the prolyl oligopeptidase (POP) family, catalyzes removal of N-terminal acetylated amino acid residues from peptides. As a key regulator of protein N-terminal acetylation, APEH was involved in many important physiological processes while its aberrant expression was correlated with progression of various diseases such as inflammation, diabetics, Alzheimer's disease (AD), and cancers. However, while emerging attention has been attracted in APEH-related disease diagnosis and drug discovery, the mechanisms behind APEH and related disease progression are still unclear; thus, further investigating the physiological role and function of APEH is of great importance.
View Article and Find Full Text PDFCharacterization of the First Marine Pestivirus, Phocoena Pestivirus (PhoPeV).
Viruses
January 2025
Institute of Virology, Department of Infectious Diseases, University of Veterinary Medicine Hannover, D-30559 Hannover, Germany.
The first marine pestivirus, Phocoena pestivirus (PhoPeV), isolated from harbor porpoise, has been recently described. To further characterize this unique pestivirus, its host cell tropism and growth kinetics were determined in different cell lines. In addition, the interaction of PhoPeV with innate immunity in porcine epithelial cells and the role of selected cellular factors involved in the viral entry and RNA replication of PhoPeV were investigated in comparison to closely and distantly related pestiviruses.
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