Adel Ghorani-Azam, Seyed Ahmad Mohajeri, Bamdad Riahi-Zanjani, Sona Sepahi, Samaneh Sepahi
Amylase is an enzyme with broad hydrolysis activities that catalyzes the hydrolysis of starch into glucose and other small molecules such as maltose. It is an enzyme of glycoside family with surface layer homology (SLH) domain. SLH, which is known as cell wall binding domain is essential for binding to peptidoglycan of cell membranes. Since designing and producing enzymes with strong catalytic activity is essential in future food industry, investigating the similarities of amylases of different species can be helpful in protein engineering of these enzymes. Homology alignment of bacterial and human amylase sequences shows that both sequences contain 511 amino acid that are highly conserved with several repeated sequences that seems to be necessary for catalysis activity and structural conformation of the protein. In this study, we aimed to characterize the most critical structural and catalytic domains of amylase using bioinformatics tools. In this study, it was shown that SLH and starch binding domain (SBD) are extremely conserved in both human and bacterial amylase. In addition, it was shown that similar domain with several repeated di- or tri-peptide sequences existed in almost all amylases indicating that these residues may have valuable functional, structural and evolutional information. The results of this study may provide new insights into biological aspects of proteins that have not yet been elucidated.