Abstract
GDSL esterase is designated as a member of Family II of lipolytic enzymes known to catalyse the synthesis and hydrolysis of ester bonds. The enzyme possesses a highly conserved motif Ser-Gly-Asn-His in the four conserved blocks I, II, III and V respectively. The enzyme characteristics, such as region-, chemo-, and enantioselectivity, help in resolving the racemic mixture of single-isomer chiral drugs. Recently, crystal structure of GDSL esterase from Photobacterium J15 has been reported (PDB ID: 5XTU) but not in complex with substrate. Therefore, GDSL in complex with substrate could provide insights into the binding mode of substrate towards inactive form of GDSL esterase (S12A) and identify the hot spot residues for the designing of a better binding pocket. Insight into molecular mechanisms is limited due to the lack of crystal structure of GDSL esterase–substrate complex. In this paper, the crystallization of mutant GDSL esterase (S12A) (PDB ID: 8HWO) and its complex with butyric acid (PDB ID: 8HWP) are reported. The optimized structure would be vital in determining hot spot residue for GDSL esterase. This preliminary study provides an understanding of the interactions between enzymes and hydrolysed p-nitro-phenyl butyrate. The information could guide in the rational design of GDSL esterase in overcoming the medical limitations associated with racemic mixture.
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Data availability
The authors confirm that the data supporting the findings of this study are available within the article. The 3D structure of the mutant GDSL S12A (PDB ID: 8HWO) and its complex form (PDB ID:8HWP). Can be accessed from Protein Data Bank (PDB).
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Acknowledgements
This work was supported by Universiti Putra Malaysia (UPM) Putra Grant (Grant no. GP/2018/9601300).
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Rahman, N.N.A., Sharif, F.M., Kamarudin, N.H.A. et al. X-ray crystallography of mutant GDSL esterase S12A of Photobacterium marinum J15. 3 Biotech 13, 128 (2023). https://doi.org/10.1007/s13205-023-03534-x
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DOI: https://doi.org/10.1007/s13205-023-03534-x