We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Characterization and Structural Insights of a Novel Arylsulfatase from Pseudoalteromonas atlantica T6c.
- Authors
Dong, Panpan; Yang, Wendi; Sun, Lifang; Jing, Dingding; Zhang, Hong; Yang, Jinbo; Wu, Linjiao; Chen, Leiqing; Wu, Yunkun
- Abstract
Arylsulfatases exhibit great potential in industry for desulfation applications, but less is known about the metallo-β-lactamase (MBL) fold arylsulfatases. To learn more about them, an MBL fold arylsulfatase from Pseudoalteromonas atlantica T6c (PaAst) was identified and characterized, and its structure was elaborated in this study. PaAst was sequence analyzed, heterologously expressed in E. coli, purified by Ni2+-NTA resin affinity chromatography and size-exclusion chromatography, functionally studied by p-nitrophenyl sulfate (pNPS), and crystallized for structure determination. The MBL fold arylsulfatase was identified by sequence analysis and confirmed by enzymatic assay on pNPS with Km 1.00 mM and Vmax 60.80 U/mg at 50 °C and pH 7.5. Furthermore, its crystals were obtained in 0.2 M sodium thiocyamate, 20% PEG3350, and its structure was determined at 2.0 Å that formed a dimer with MBL fold. Our work highlighted the MBL fold arylsulfatases from structural insights and could be the theoretical foundation for investigations into their catalytic mechanism.
- Subjects
ARYLSULFATASES; ESCHERICHIA coli; AFFINITY chromatography; ENZYMATIC analysis; SEQUENCE analysis
- Publication
Catalysts (2073-4344), 2023, Vol 13, Issue 4, p759
- ISSN
2073-4344
- Publication type
Article
- DOI
10.3390/catal13040759