Related Experiment Video
Updated: May 29, 2025

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Mining and Modification of Key Functional Regions of the Nattokinase Propeptide
Aixia Ma1, Hong Wang2, Huiyang Jia2
1Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi 830017, China.
Abstract:
The nattokinase propeptide acts as an intramolecular chaperone that is essential for the correct folding of the mature peptide. Understanding key catalytic regions and sites in this propeptide is crucial for enhancing the nattokinase folding efficiency. Through bioinformatics and enzyme activity screening, we pinpointed critical sites affecting folding efficiency and identified mutants Y106V and A103T. In fermentation, their crude enzyme activities reached 277.83 and 205.63% of those of WT, respectively. Mutant Y106V exhibited a 19.2% increase in the specific enzyme activity, improving both the folding efficiency and peptide conformation. Molecular dynamics simulations elucidated the catalytic changes in Y106V and A103T. Optimization of fermentation processes for these mutants yielded nattokinase levels of 317.042 and 336.65 U/mL. This study lays a foundation for further research on nattokinase propeptide function and modification.
Related Concept Videos
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Regulation of Nuclear Protein Sorting
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....

