Structural highlights
Function
Q8A4M9_BACTN
Publication Abstract from PubMed
Glutamate decarboxylase catalyzes the conversion of glutamate to gamma-aminobutyric acid, which plays a vital role in the gut-brain axis. Herein, a novel glutamate decarboxylase from Bacteroides thetaiotaomicron (BTGAD) was heterologously expressed. BTGAD possessed high catalytic efficiency at 60â and pH 3.6. As pH response, N-terminal sequence (NTS), C-terminal sequence (CTS), and beta-hairpin in BTGAD coordinately regulated its activity under different pH. NTS folded into a loop under acidic pH, and the truncation of NTS severely reduced its activity to 4.2%. While CTS occupied the active site under neutral pH and became disordered to release the inhibition effect under acidic conditions. The beta-hairpin, located near the active site, swung and formed open and closed conformations, which acted as an activity switch. This study provides the molecular basis for the coordinated regulation mechanism of BTGAD and lays a theoretical foundation for understanding the metabolism of dietary glutamate and its interaction relationships with the gut-brain axis.
Coordinated regulation of Bacteroides thetaiotaomicron glutamate decarboxylase activity by multiple elements under different pH.,Liu S, Wen B, Du G, Wang Y, Ma X, Yu H, Zhang J, Fan S, Zhou H, Xin F Food Chem. 2023 Mar 1;403:134436. doi: 10.1016/j.foodchem.2022.134436. Epub 2022 , Sep 28. PMID:36358099[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu S, Wen B, Du G, Wang Y, Ma X, Yu H, Zhang J, Fan S, Zhou H, Xin F. Coordinated regulation of Bacteroides thetaiotaomicron glutamate decarboxylase activity by multiple elements under different pH. Food Chem. 2023 Mar 1;403:134436. PMID:36358099 doi:10.1016/j.foodchem.2022.134436
