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Purification and characterization of the Escherichia coli thermoresistant gluconokinase encoded by the gntK gene
Author(s) -
Izu Hanae,
Adachi Osao,
Yamada Mamoru
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00923-4
Subject(s) - escherichia coli , enzyme , gene , biochemistry , biology , dimer , function (biology) , chemistry , microbiology and biotechnology , genetics , organic chemistry
A thermoresistant gluconokinase encoded by the gntK gene of Escherichia coli K‐12 was purified and characterized. The K m values of the purified enzyme for gluconate and ATP are 42 μM and 123 μM, respectively, and the activity was not altered by the presence of pyruvate. The enzyme was shown to function as a dimer with two identical subunits of 18.4 kDa. These characteristics appear to be distinct from those of the gluconokinase reported by E.I. Vivas, A. Liendo, K. Dawidowicz, and T. Istúriz (1994) J. Basic. Microbiol. 16, 117–122.