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• W2163568009 endingPage "2211" @default.
• W2163568009 startingPage "2206" @default.
• W2163568009 abstract "ABSTRACT The gene for a novel α-amylase, designated AmyC, from the hyperthermophilic bacterium Thermotoga maritima was cloned and heterologously overexpressed in Escherichia coli . The putative intracellular enzyme had no amino acid sequence similarity to glycoside hydrolase family (GHF) 13 α-amylases, yet the range of substrate hydrolysis and the product profile clearly define the protein as an α-amylase. Based on sequence similarity AmyC belongs to a subgroup within GHF 57. On the basis of amino acid sequence similarity, Glu185 and Asp349 could be identified as the catalytic residues of AmyC. Using a 60-min assay, the maximum hydrolytic activity of the purified enzyme, which was dithiothreitol dependent, was found to be at 90°C. AmyC displayed a remarkably high pH optimum of pH 8.5 and an unusual sensitivity towards both ATP and EDTA." @default.
• W2163568009 created "2016-06-24" @default.
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• W2163568009 date "2006-03-01" @default.
• W2163568009 modified "2023-09-28" @default.
• W2163568009 title "Identification and Characterization of a Novel Intracellular Alkaline α-Amylase from the Hyperthermophilic Bacterium <i>Thermotoga maritima</i> MSB8" @default.
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• W2163568009 doi "https://doi.org/10.1128/aem.72.3.2206-2211.2006" @default.
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