Prospective identification of extracellular triacylglycerol hydrolase with conserved amino acids in Amycolatopsis tolypomycina's high G+C genomic dataset
Issued Date
2025-03-01
Resource Type
eISSN
2215017X
Scopus ID
2-s2.0-85211480387
Journal Title
Biotechnology Reports
Volume
45
Rights Holder(s)
SCOPUS
Bibliographic Citation
Biotechnology Reports Vol.45 (2025)
Suggested Citation
Sraphet S., Javadi B. Prospective identification of extracellular triacylglycerol hydrolase with conserved amino acids in Amycolatopsis tolypomycina's high G+C genomic dataset. Biotechnology Reports Vol.45 (2025). doi:10.1016/j.btre.2024.e00869 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/102773
Title
Prospective identification of extracellular triacylglycerol hydrolase with conserved amino acids in Amycolatopsis tolypomycina's high G+C genomic dataset
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Abstract
Extracellular triacylglycerol hydrolases (ETH) play a critical role for microorganisms, acting as essential tools for lipid breakdown and survival in challenging environments. The pursuit of more effective ETH genes and enzymes through evolution holds significant potential for enhancing living conditions. This study employs a proteogenomic approach to identify high G+C ETH in a notable Gram-positive bacterium, Amycolatopsis tolypomycina. Utilizing knowledge from genome and machine learning algorithms, prospective ETH genes/enzymes were identified. Notably, the ETH structural conserved accessibility to solvent clearly indicated the specific sixteen residues (GLY50, PRO93, GLY141, ASP148, GLY151, ASP172, ALA176, GLY195, TYR196, SER197, GLN198, GLY199, GLY200, GLY225, PRO327, ASP336) with no frequency. By pinpointing key residues and understanding their role, this study sets the stage for enhancing ETH performance through computational proteogenomic and contributes to the broader field of enzyme engineering, facilitating the development of more efficient and versatile ETH enzymes tailored to specific industrial or environmental contexts.