Structural highlights
FunctionPublication Abstract from PubMedPaaY is a thioesterase that enables toxic metabolites to be degraded through the bacterial phenylacetic acid (PA) pathway. The Acinetobacter baumannii gene FQU82_01591 encodes PaaY, which we demonstrate to possess gamma-carbonic anhydrase activity in addition to thioesterase activity. The crystal structure of AbPaaY in complex with bicarbonate reveals a homotrimer with a canonical gamma-carbonic anhydrase active site. Thioesterase activity assays demonstrate a preference for lauroyl-CoA as a substrate. The AbPaaY trimer structure shows a unique domain-swapped C-termini, which increases the stability of the enzyme in vitro and decreases its susceptibility to proteolysis in vivo. The domain-swapped C-termini impact thioesterase substrate specificity and enzyme efficacy without affecting carbonic anhydrase activity. AbPaaY knockout reduced the growth of Acinetobacter in media containing PA, decreased biofilm formation, and impaired hydrogen peroxide resistance. Collectively, AbPaaY is a bifunctional enzyme that plays a key role in the metabolism, growth, and stress response mechanisms of A. baumannii. Mechanistic and structural insights into the bifunctional enzyme PaaY from Acinetobacter baumannii.,Jiao M, He W, Ouyang Z, Qin Q, Guo Y, Zhang J, Bai Y, Guo X, Yu Q, She J, Hwang PM, Zheng F, Wen Y Structure. 2023 Aug 3;31(8):935-947.e4. doi: 10.1016/j.str.2023.05.015. Epub 2023 , Jun 16. PMID:37329879[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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