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BMB Rep. 2009 Jun 30;42(6):350-5.

Enzymatic properties of the N- and C-terminal halves of human hexokinase II.

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Division of Nuclear Medicine, Department of Diagnostic Radiology, Research Institute of Radiological Science, Yonsei University College of Medicine, Seoul 120-752, Korea.


Although previous studies on hexokinase (HK) II indicate both the N- and C-terminal halves are catalytically active, we show in this study the N-terminal half is significantly more catalytic than the C-terminal half in addition to having a significantly higher Km for ATP and Glu. Furthermore, truncated forms of intact HK II lacking its first N-terminal 18 amino acids (delta18) and a truncated N-terminal half lacking its first 18 amino acids (delta18N) have higher catalytic activity than other mutants tested. Similar results were obtained by PET-scan analysis using (18)FFDG. Our results collectively suggest that each domain of HK II possesses enzyme activity, unlike HK I, with the N-terminal half showing higher enzyme activity than the C-terminal half.

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