Functional cloning and predictive structural modeling of a novel esterase from Bacillus subtilis strain, RRL 1789

The Journal of General and Applied Microbiology

Nishawar Jan¹  Khurshid I. Andrabi¹  Mahboob Ul Hussain¹  Ghulam N. Qazi²  Vijeshwar Verma²  Kaiser Peerzada¹ 

[1] Department of Biotechnology, University of Kashmir;Indian Institute of Integrative Medicine (IIIM)

关键词: bacillus;    cloning;    esterases;    genomic library;   

DOI  :  10.2323/jgam.55.317

学科分类：微生物学和免疫学

来源: Applied Microbiology, Molecular and Cellulrar Biosciences Research Foundation

【 摘 要 】

We have recently reported the purification and characterization of a novel esterase from the Bacillus subtilis strain. In the present study we report the genomic DNA cloning and predictive structural modeling of this novel esterase. Tributyrin- and Rhodamine B-based functional screen of a Bacillus subtilis genomic library led to the identification of a potential lipolytic gene. DNA sequence analysis of the cloned gene showed that it encodes a protein of 489 amino acid residues. Sequence homology search and multiple sequence alignment showed that the protein was highly homologous to known esterases. Secondary structure-driven multiple sequence alignment with the homologous esterase of known three-dimensional structures was performed and a 3D structure model of this enzyme was constructed. Based on the topological organization of the secondary structures, this protein belongs to the α/β hydrolase superfamily. Moreover, the presence of serine in the context of amino acid sequence G/A-X-S-X-G (with X an arbitary amino acid residue) in the protein indicates that it belong to the class of serine hydrolases of this superfamily.

【 授权许可】

Unknown