PMID:8014844
| Citation |
Vivas, EI, Liendo, A, Dawidowicz, K and Istúriz, T (1994) Isolation and characterization of the thermoresistant gluconokinase from Escherichia coli. J. Basic Microbiol. 34:117-22 |
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| 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. |
| Links | |
| Keywords |
Escherichia coli/enzymology; Kinetics; Molecular Weight; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Phosphotransferases (Alcohol Group Acceptor)/isolation & purification; Phosphotransferases (Alcohol Group Acceptor)/metabolism; Temperature |
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