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- W2036148552 abstract "It is known that two gluconokinases are inducibly expressed during the utilization of gluconate by E. coli. One is thermoresistant (activity stable for 3 h at 30 degrees C) and the other thermosensitive (losses 75% or more of its activity under the above conditions). The thermoresistant gluconokinase (EC 2.7.1.12) was isolated, purified and characterized for the first time from the E. coli mutant Ca26, a K12 derivative which lacks the thermosensitive activity. The enzyme was purified 43 fold with a recovery of 11%. The M(r) of the enzyme was 100 kDa with three equal subunits of approximately 29.5 kDa. The enzyme exhibited Michaelis-Menten kinetics and the Km values for gluconate and ATP were 0.02 mM and 0.045 mM respectively." @default.
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- W2036148552 date "1994-01-01" @default.
- W2036148552 modified "2023-09-27" @default.
- W2036148552 title "Isolation and characterization of the thermoresistant gluconokinase fromEscherichia coli" @default.
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- W2036148552 doi "https://doi.org/10.1002/jobm.3620340207" @default.
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