9kov
From Proteopedia
Crystal structure of an amidohydrolase mutant from Thermonema
Structural highlights
Publication Abstract from PubMedOchratoxin A (OTA) is highly toxic and widely distributed, posing serious threats to human and animal health. Searching for effective OTA-detoxifying enzyme is crucial for the prevention and control of OTA contaminations. Here, a new OTA-detoxifying enzyme, TrADH from Thermonema rossianum is identified, which exhibits highest temperature tolerance among OTA-detoxifying enzymes. TrADH maintains good activity in the range of 45-85 degrees C and retains about 50 % activity after heating at 70 degrees C for 30 min. Based on the solved crystal structures, the catalytic mechanism is proposed, and protein engineering of catalytic-related residues is performed to obtain a 2.1-fold upgraded variant TrADHS67E with the specific enzyme activity of 3990 U/mg, which is more efficient than the reported OTA-detoxifying enzymes. The efficient degradation of OTA in rum and walnut reveals the prospect of TrADH in food applications. The results indicate that TrADH has the potential in OTA bio-detoxification in food and feed industry. A thermostable OTA-detoxifying hydrolase from Thermonema rossianum: identification, characterization, structure, catalytic mechanism, and application.,Xu N, Yan M, Liang X, Qin H, Gao J, Liu W Food Chem. 2025 Sep 1;485:144515. doi: 10.1016/j.foodchem.2025.144515. Epub 2025 , Apr 25. PMID:40318335[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
Categories: Large Structures | Pyrinomonas methylaliphatogenes | Chen YY | Han X | Jian G | Liu W | Wei HL | Wu P | Xu NN
