X-ray crystallography of mutant GDSL esterase S12A of Photobacterium marinum J15

X-ray crystallography of mutant GDSL esterase S12A of Photobacterium marinum J15

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 regio...

Full description

Saved in:
Bibliographic Details
Published in:3 Biotech Vol. 13; no. 5; p. 128
Main Authors: Rahman, Nor Najihah Abdul, Sharif, Fairolniza Mohd, Kamarudin, Nor Hafizah Ahmad, Ali, Mohd Shukuri Mohamad, Aris, Sayangku Nor Ariati Mohamad, Jonet, Mohd Anuar, Rahman, Raja Noor Zaliha Raja Abd, Sabri, Suriana, Leow, Thean Chor
Format: Journal Article
Language:English
Published: Cham Springer International Publishing 01-05-2023
Springer Nature B.V
Subjects:
Agriculture
Binding
Bioinformatics
Biomaterials
Biotechnology
Butyric acid
Cancer Research
Chemical synthesis
Chemistry
Chemistry and Materials Science
Conserved sequence
Crystal structure
Crystallization
Crystallography
Enantiomers
Enzymes
Esterase
Mixtures
Molecular modelling
Mutants
Original
Original Article
Photobacterium
Residues
Stem Cells
Substrates
X-ray crystallography
GDSL esterase
Racemic mixture
Regiospecificity
Binding pocket
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:2190-572X
2190-5738
DOI:10.1007/s13205-023-03534-x