Abstract
Computational analysis of amino acid sequences of aliphatic amidases and kynurenine formamidases for some of their physiochemical properties and their substrate specificity has been done. Multiple sequence alignment of 18 amino acid sequences shows a clear difference between the two classes of aminohydrolases. Statistical analysis indicated a clear distinction between aliphatic amidases and kynurenine formamidases. The kynurenine formamidases and aliphatic amidases mainly differ in the total number of amino acid and composition of amino acid. Catalytic triad was found to be conserved and difference in amino acids makes them substrate specific. The results of the present work will be quite useful in prediction and selection of kynurenine formamidases/aliphatic amidases either from reported amidases or from the large number of sequenced microbial genome. Key words: Aliphatic amidases, kynurenine formamidases, amino acids, substrate specificity, multiple alignments
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