title: Structure prediction and functional analyses of a thermostable lipase obtained from Shewanella putrefaciens.
abstract: Previous experimental studies on thermostable lipase from Shewanella putrefaciens suggested the maximum activity at higher temperatures, but with little information on its conformational profile. In this study, the three-dimensional structure of lipase was predicted and a 60 ns molecular dynamics (MD) simulation was carried out at temperatures ranging from 300 to 400 K to better understand its thermostable nature at the molecular level. MD simulations were performed in order to predict the optimal activity of thermostable lipase. The results suggested strong conformational temperature dependence. The thermostable lipase maintained its bio-active conformation at 350 K during the 60 ns MD simulations.
authors.affiliation: a School of Chemistry and Chemical Engineering , Henan University of Technology , Zhengzhou 450001 , Henan , China.
authors.forename: Faez Iqbal
authors.identifier: http://orcid.org/0000-0001-9088-0723
authors.initials: FI
authors.lastname: Khan
authors.affiliation: b School of Pharmacy and Pharmacology , University of KwaZulu-Natal , Durban 4000 , South Africa.
authors.forename: Bilal
authors.initials: B
authors.lastname: Nizami
authors.affiliation: c Department of Anatomy (Microbiology) , Al-Imam Muhammad Ibn Saud Islamic University , Riyadh , Saudi Arabia.
authors.forename: Razique
authors.initials: R
authors.lastname: Anwer
authors.affiliation: a School of Chemistry and Chemical Engineering , Henan University of Technology , Zhengzhou 450001 , Henan , China.
authors.forename: Ke-Ren
authors.initials: KR
authors.lastname: Gu
authors.affiliation: d Department of Chemistry , Durban University of Technology , Durban 4000 , South Africa.
authors.forename: Krishna
authors.initials: K
authors.lastname: Bisetty
authors.affiliation: e Centre for Interdisciplinary Research in Basic Science, Jamia Millia Islamia , New Delhi 110025 , India.
authors.forename: Md Imtaiyaz
authors.identifier: http://orcid.org/0000-0002-3663-4940
authors.initials: MI
authors.lastname: Hassan
authors.affiliation: a School of Chemistry and Chemical Engineering , Henan University of Technology , Zhengzhou 450001 , Henan , China.
authors.forename: Dong-Qing
authors.initials: DQ
authors.lastname: Wei
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D004795:Enzyme Stability; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology; D004950:Esterases / Q000737:chemistry*; D006358:Hot Temperature; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010713:Phosphatidylcholines / Q000737:chemistry*; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D016415:Sequence Alignment; D020614:Shewanella putrefaciens / Q000737:chemistry* / Q000201:enzymology; D040681:Structural Homology, Protein; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D010713:Phosphatidylcholines; D004950:Esterases; D008049:Lipase; C428386:thermostable lipase; C017251:1,2-oleoylphosphatidylcholine
keywords: MD simulations; lipase; structure prediction; thermostability