Source:http://linkedlifedata.com/resource/pubmed/id/19558793
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2009-6-29
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1976-6696
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
350-5
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pubmed:meshHeading |
pubmed-meshheading:19558793-Catalysis,
pubmed-meshheading:19558793-Catalytic Domain,
pubmed-meshheading:19558793-Hexokinase,
pubmed-meshheading:19558793-Humans,
pubmed-meshheading:19558793-Isoenzymes,
pubmed-meshheading:19558793-Kinetics,
pubmed-meshheading:19558793-Mutant Proteins,
pubmed-meshheading:19558793-Protein Structure, Tertiary,
pubmed-meshheading:19558793-Tumor Cells, Cultured
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pubmed:year |
2009
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pubmed:articleTitle |
Enzymatic properties of the N- and C-terminal halves of human hexokinase II.
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pubmed:affiliation |
Division of Nuclear Medicine, Department of Diagnostic Radiology, Research Institute of Radiological Science, Yonsei University College of Medicine, Seoul 120-752, Korea.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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