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

Authors
 Keun Jae Ahn  ;  Jongsun Kim  ;  Mijin Yun  ;  Jeon Han Park  ;  Jong Doo Lee 
Citation
 BMB Reports, Vol.42(6) : 350-355, 2009 
Journal Title
 BMB Reports 
ISSN
 1976-6696 
Issue Date
2009
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
Files in This Item:
T200902184.pdf Download
DOI
10.5483/BMBRep.2009.42.6.350
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Dermatology (피부과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Nuclear Medicine (핵의학교실) > 1. Journal Papers
Yonsei Authors
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
Park, Jeon Han(박전한) ORCID logo https://orcid.org/0000-0001-9604-3205
Ahn, Keun Jae(안근재)
Yun, Mi Jin(윤미진) ORCID logo https://orcid.org/0000-0002-1712-163X
Lee, Jong Doo(이종두)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/104059
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