title: Activation of Candida rugosa lipase at alkane-aqueous interfaces: a molecular dynamics study.
abstract: The effect of solvent hydrophobicity on activation of Candida rugosa lipase (CRL) was investigated by performing molecular dynamics simulations for four nano seconds (ns). The closed/inactive conformer of CRL (PDB code 1TRH) was solvated in three alkane-aqueous environments. The alkanes aggregated in a predominantly aqueous environment and by 1 ns a stable spherical alkane-aqueous interface had formed. This led to the interfacial activation of CRL. On analyzing the simulated conformers with the closed conformer of CRL, the flap was found to have opened from a closed state by 7.7 A, 10.2 A, 13.1 A at hexane-aqueous, octane-aqueous, and decane-aqueous interfaces. Further, essential dynamics analysis revealed that major anharmonic fluctuations were confined to residues 64-81, the flap of CRL.
authors.affiliation: Centre for Biotechnology, Anna University, Chennai 600025, India.
authors.forename: Jayasundar Jayant
authors.initials: JJ
authors.lastname: James
authors.forename: Baddireddi Subadhra
authors.initials: BS
authors.lastname: Lakshmi
authors.forename: Aswin Sai Narain
authors.initials: AS
authors.lastname: Seshasayee
authors.forename: Pennathur
authors.initials: P
authors.lastname: Gautam
mesh_terms: D000473:Alkanes / Q000737:chemistry*; D002175:Candida / Q000201:enzymology*; D003198:Computer Simulation; D004789:Enzyme Activation; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014867:Water / Q000737:chemistry
chemical_list: D000473:Alkanes; D005656:Fungal Proteins; D014867:Water; D008049:Lipase; C012867:decane