In silico analysis of some microbial amidases for their amino acid and physiochemical parameters

摘要: Amino acid sequences of amidases were retrieved from respective databases and in silico analysis for different physiochemical properties substrate specificity has been done. Multiple Sequence Alignment (MSA) statistical amino revealed significant differences among aliphatic signature terms conserved motif that plays a vital role binding catalytic function. MSA the residues involved function are position specific which remains within traid Cys-166, Glu-59, Lys-134, while amidase contains GGSS (S/G) GS Ser-171, Ser-195, Lys-96 not specific. Statistical these two groups also differ properties. In contrast to amidases, have significantly higher number & molecular mass, theoretical pI, charged (negative positive) residues, index grand average hydropathicity. Present investigation i.e. Cys, Met, Tyr, Asn, Ile, Trp, Glu Gly case acids i.e Leu, Pro, Ser, Ala Val found play an important both enzyme catalysis, as well structural stability.