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- W2186794241 abstract "Enzyme's active site sequence is crucial to execute its function. The present study is based on the analysis of comparative frequency distribution of enzymes catalytic residues belongs to different organisms and localizations. The frequency distribution of enzymes catalytic residues was computed using the number of amino acids of each type and the total number of residues. The percentage composition of catalytic residue indicates the occurrence of 13 amino acids (out of 20 total amino acids) at enzymatic active site. These 13 catalytic residues are cumulatively constituted by five charged (E, D, H, K, R), six polar (C, Y, T, S, Q, N) and two hydrophobic residues (A/F/W, G). Viral, Prokaryotic and Eukaryotic enzymes (VEs, pEs and eEs) commonly show preference for four charged residues (H, D, E, R) and a single polar residue 'S' at their active site. The residues 'R>A' are predominantly distributed at VEs active site, while in pEs and eEs the order of preference of catalytic residues is H>D>K>E>R>Y>S. The analysis further indicate that both Prokaryotic and Eukaryotic membrane and non-membrane enzymes (MEs and nMEs) show high degree of similarity in the overall percentage distribution of charged and polar residues at their active site. In addition, VEs are significantly similar to nMEs in the frequency distribution of charged and polar residues. The catalytic residues 'H, D, S, Y, T, F' play crucial role in the catalysis of Prokaryotic membrane enzymes (pMEs), while the residues 'H, K, Y, S, C' are important for Eukaryotic membrane enzymes (eMEs) catalysis. However, in non-membrane enzymes (nMEs) five charged residues (E, D, H, K, R) are important for their catalytic function, while the polar residues have supportive function. The knowledge of amino acid frequency distribution at the active site can be exploited in designing novel enzyme active sites as well as the specific inhibitors and novel peptide based drugs." @default.
- W2186794241 created "2016-06-24" @default.
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- W2186794241 date "2011-01-01" @default.
- W2186794241 modified "2023-09-27" @default.
- W2186794241 title "AMINO ACID FREQUENCY DISTRIBUTION AT ENZYMATIC ACTIVE SITE" @default.
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