Year: 2009
Type: article
Abstract: 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.
Source: BMB Reports
Authors: Keun-Jae Ahn, Jong-Sun Kim, Mi-Jin Yun, Jeon-Han Park, Jong-Doo Lee
Language: English
Subfield: Cancer Research
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $550
OpenAlex ID: W2057075868