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KMID : 0624620090420060350
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BMB Reports
2009 Volume.42 No. 6 p.350 ~ p.355
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Enzymatic properties of the N- and C-terminal halves of human hexokinase II
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Ahn Keun-Jae
Park Jeon-Han
Kim Jong-Sun
Lee Jong-Doo
Yun Mi-Jin
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Abstract
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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 (Δ18) and a truncated N-terminal half lacking its first 18 amino acids (Δ18N) have higher catalytic activity than other mutants tested. Similar results were obtained by PET-scan analysis using 18FFDG. 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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KEYWORD
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Conformation, Deletion mutant, Hexokinase II, Kinetics properties, 18F-FDG
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