Thermostable chitinase II from Thermomyces lanuginosus SSBP : Cloning, structure prediction and molecular dynamics simulations
Khan, Faez Iqbal
MetadataShow full item record
Copyright: 2015. Elsevier. Due to copyright restrictions, only the abstract is available. For access to the full text item, please consult the publisher's website. The definitive version of the work is published in Journal of Theoretical Biology. Vol. 374 . pp 107-114.
Thermomyces lanuginosus is a thermophilic fungus that produces large number of industrially-signiﬁcant enzymes owing to their inherent stability at high temperatures and wide range of pH optima, including thermostable chitinases that have not been fully characterized. Here, we report cloning, characterization and structure prediction of a gene encoding thermostable chitinase II. Sequence analysis revealed that chitinase II gene encodes a 343 amino acid protein of molecular weight 36.65 kDa. Our study reports that chitinase II exhibits a well-deﬁned TIM-barrel topology with an eight-stranded α/β domain. Structural analysis and molecular docking studies suggested that Glu176 is essential for enzyme activity. Folding studies of chitinase II using molecular dynamics simulations clearly demonstrated that the stability of the protein was evenly distributed at 350 K.
Khan, F. I. et al. 2015. Thermostable chitinase II from Thermomyces lanuginosus SSBP: Cloning, structure prediction and molecular dynamics simulations. Journal of Theoretical Biology, 374: 107-114.