Purification and characterization of the Escherichia coli thermoresistant glucokinase encoded by the gntK gene.
A thermoresistant gluconokinase encoded by the gntK gene of Escherichia coli K-12 was purified and characterized. The Km values of the purified enzyme for gluconate and ATP are 42 microM and 123 microM, 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.
Izu
H
H
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Japan.
Adachi
O
O
Yamada
M
M
D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D007700:Kinetics; D008970:Molecular Weight; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011487:Protein Conformation; D019289:Pyruvic Acid / Q000494:pharmacology; D013696:Temperature
D019289:Pyruvic Acid; D017853:Phosphotransferases (Alcohol Group Acceptor); C020578:gluconokinase