8HEA

Esterase2 (EaEst2) from Exiguobacterium antarcticum

Summary for 8HEA

• Entry DOI: 10.2210/pdb8hea/pdb
• Descriptor: Thermostable carboxylesterase Est30 (2 entities in total)
• Functional Keywords: esterase, hydrolase
• Biological source: Exiguobacterium antarcticum B7
• Total number of polymer chains: 1
• Total formula weight: 27727.58

Authors

Hwang, J.,Lee, J.H. (deposition date: 2022-11-08, release date: 2023-09-20)

Primary citation

Hwang, J.,Yoo, W.,Shin, S.C.,Kim, K.K.,Kim, H.W.,Do, H.,Lee, J.H.
Structural and Biochemical Insights into Bis(2-hydroxyethyl) Terephthalate Degrading Carboxylesterase Isolated from Psychrotrophic Bacterium Exiguobacterium antarcticum.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: This study aimed to elucidate the crystal structure and biochemically characterize the carboxylesterase Est2, a thermotolerant biocatalyst derived from , a psychrotrophic bacterium. Sequence and phylogenetic analyses showed that Est2 belongs to the Family XIII group of carboxylesterases. Est2 has a broad range of substrate specificities for short-chain -nitrophenyl (NP) esters, 1-naphthyl acetate (1-NA), and 1-naphthyl butyrate (1-NB). Its optimal pH is 7.0, losing its enzymatic activity at temperatures above 50 °C. Est2 showed degradation activity toward bis(2-hydroxyethyl) terephthalate (BHET), a polyethylene terephthalate degradation intermediate. We determined the crystal structure of Est2 at a 1.74 Å resolution in the ligand-free form to investigate BHET degradation at a molecular level. Finally, the biochemical stability and immobilization of a crosslinked enzyme aggregate (CLEA) were assessed to examine its potential for industrial application. Overall, the structural and biochemical characterization of Est2 demonstrates its industrial potency as a biocatalyst.

PubMed: 37569396
DOI: 10.3390/ijms241512022

Experimental method

X-RAY DIFFRACTION (1.74 Å)