The structural insights of L-asparaginase from <i>Pseudomonas aeruginosa</i> CSPS4 at elevated temperatures highlight its thermophilic nature.

ABSTRACT: In the present investigation, a novel thermophilic L-asparaginase (Asn_PA) from Pseudomonas aeruginosa CSPS4 was investigated to explore its structural insights at elevated temperatures. Sequence analysis of Asn_PA depicted three conserved motifs (VVILATGGTIAG, DGIVITHGTDTLEETAYFL, and, LRKQGVQIIRSSHVNAGGF), of them, two motifs exhibit catalytically-important residues i.e., T⁴⁵ and T¹²⁵. A homology modelling-based structure model for Asn_PA was generated with 4PGA as the top-matched template. The predicted structure was validated and energy was minimized. Molecular docking was carried out cantered at the active site for asparagine and glutamine as its substrate ligands. The enzyme-substrate interaction analysis showed binding affinities of  - 4.8 and  - 4.1 kca

SUBMITTER: Kumar V 

PROVIDER: S-EPMC11391003 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature