Affiliations: Department of Biotechnology, Indian Institute of
Technology Guwahati, Assam, India
Note:  Corresponding author: Dr. Sanjukta Patra, Department of
Biotechnology, Indian Institute of Technology, Guwahati- 781039, Assam, India.
Tel.: +91 361 2582213; Fax: +91 361 2582249; E-mail: email@example.com
Abstract: Bacterial true lipases having thermo and alkaline stability are
highly attractive for their industrial production of pharmaceuticals,
agrochemicals, cosmetics, and flavour. Staphylococcus aureus lipase
(SAL3) remains active at temperatures 40–60°C, with
an optimum temperature of 55°C and an optimum pH of
9.5 stable over a range of 5–12. Detailed understanding of the structure and
insight into the activity of such lipase would aid in engineering lipases that
would function in the desired extreme industrial environments. In the present
study, we carried out in silico characterization and structural modeling
of SAL3 which is thermoactive, alkaline and detergent-stable. Comparison of
SAL3 with other staphylococcal lipases indicates that SAL3 is a true
lipase having the catalytic triad (residues Ser119, Asp310 & His352) and
the calcium binding site (residues Asp351, Asp354, Asp359, Asp362 and Gly286).
Conservation in sequence implies that interfacial activation mechanism is
possible in SAL3 with the lid formed by helix (residues 180–196) and loop
(residues 197–206). Three dimensional (3D) structure model of SAL3 has been
predicted for the first time and aims at understanding its function and
biochemical characteristics of possessing relatively high thermal and pH stability.