Insilco Homology Structure and Functional Site Prediction Studies on Collagenase Protein in Fiddler Crab


Shoba.K, Assistant Professor, Moganapriya S, Research Scholar
Department of Biochemistry and Biotechnology, D. K. M. College For Women (Autonomous), Vellore, Tamilnadu, India.


Enzymes are used in a variety of industrial processes to create an array of foods, cosmetics and pharmaceuticals. They offer advantages over chemical techniques including substrate specificity and elevated activity that allow better control of the production processes. However, the use of enzymes in industrial applications requires their large scale production. There are a few enzymes that breakdown collagen other than collagenase (cathepsin K and elastase), but collagenase enzymes (serine collagenase and metallocollagenase) are specific enzymes for collagen. They are particularly attractive because they do not require special conditions to break down the substrate. Collagenase enzyme can be isolated from digestive organs of different fish and invertebrates. They are secreted as latent form that can be activated with a member of different material that converts it to the active form. 4-Aminophenylmercuric Acetate (APMA) is the most commonly used but trypsin, Dithiothreitol (DTT) and other activators (potassium or sodium thiocyanate) have been used. On the other hand, Ethylenediaminetetraacetic Acid (EDTA), mercaptoethanol, O-phenanthroline and cysteine have similar mechanisms to inactivate collagenases. Collagenase enzymes are effective at physiological pH (6-8) and a wide range of temperature (20-40°C). Using pattern searching method, motif and domain region of collagenase proteins has been predicted. Studies on gene profiling using a review show the functional part of the target gene.3D structure of collagenase proteins were modeled by using CPH server.