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• W2040340248 abstract "The L-asparaginase from an extreme thermophile, Thermus aquaticus strain T351, was highly substrate- and stereospecific, with no activity against glutamine or D-asparagine. It had a high Km of 8.6 mM. In these aspects it closely resembled the corresponding enzymes from thermophilic bacteria. The enzyme had a molecular weight of 80,000, an isoelectric point of 4.6, and a pH optimum of 9.5. It showed some substrate inhibition above 20 mM asparagine and was also inhibited by L-aspartic acid, D- and L-lysine (Ki of 5.2 and 1.25 mM, respectively), and D- and L-serine. The half-life of the enzyme at 85 degrees C was 40 min. The Arrhenius plot showed a change in slope at 55 degrees C." @default.
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• W2040340248 date "1985-09-01" @default.
• W2040340248 modified "2023-10-09" @default.
• W2040340248 title "A specific l-asparaginase from Thermus aquaticus" @default.
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• W2040340248 doi "https://doi.org/10.1016/0003-9861(85)90582-x" @default.
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