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Isolation and characterization of the thermoresistant gluconokinase from Escherichia coli

✍ Scribed by Eugenio I. Vivas; Andreina Liendo; Karl Dawidowicz; Tomás Istúriz

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
423 KB
Volume
34
Category
Article
ISSN
0233-111X

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✦ Synopsis

It is known that two gluconokinases are inducibly expressed during the utilization of gluconate by E. coli. One is therrnoresistant (activity stable for 3 h at 30 "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, of the enzyme was 100 kDa with three equal subunits of approxirnatcly 29.5 kDa. The enzyme exhibited MICHAELIS-MENTEN kinetics and the K, values for gluconate and ATP were 0.02 r n M and 0.045 mM respectively.

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