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• W2078384073 endingPage "507" @default.
• W2078384073 startingPage "491" @default.
• W2078384073 abstract "A comparative study of amino acid sequence and physicochemical properties indicates the affiliation of protein from the nitrilase/cyanide hydratase family. This family contains nitrilases that break carbon–nitrogen bonds and appear to be involved in the reduction of organic nitrogen compounds and ammonia production. They all have distinct substrate specificity and include nitrilase, cyanide hydratases, aliphatic amidases, beta-alanine synthase, and a few other proteins with unknown molecular function. These sequences were analyzed for different physical and chemical properties and to relate these observed differences to the thermostability properties, phylogenetic tree construction and the evolutionary relationship among them. In this work, in silico analysis of amino acid sequences of mesophilic (15) and thermophilic (archaea, 15 and bacteria, 15) proteins has been done. The physiochemical properties of these three groups of nitrilase/cyanide hydratase family also differ in number of amino acids, molecular weight, pI values, positively charged ions, i.e. Arg + Lys, aliphatic index and grand average of hydropathacity (GRAVY). The amino acid Ala (1.37-fold) was found to be higher in mesophilic bacteria as compared to thermophilic bacteria but Lys and Phe were found to be significantly high (1.43 and 1.39-fold, respectively) in case of thermophilic bacteria. The amino acids Ala, Cys, Gln, His and Thr were found to be significantly higher (1.41, 1.6, 1.77, 1.44 and 1.29-fold, respectively) in mesophilic bacteria as compared to thermophilic archaea, where Glu, Leu and Val were found significantly high (1.22, 1.19 and 1.26-fold, respectively)." @default.
• W2078384073 created "2016-06-24" @default.
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• W2078384073 creator A5068116243 @default.
• W2078384073 creator A5081938985 @default.
• W2078384073 date "2013-01-16" @default.
• W2078384073 modified "2023-10-18" @default.
• W2078384073 title "Comparative analysis of amino acid sequences from mesophiles and thermophiles in respective of carbon–nitrogen hydrolase family" @default.
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• W2078384073 doi "https://doi.org/10.1007/s13205-012-0111-3" @default.
• W2078384073 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3824785" @default.
• W2078384073 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28324422" @default.
• W2078384073 hasPublicationYear "2013" @default.
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