Linked Life Data

19558793

Source:http://linkedlifedata.com/resource/pubmed/id/19558793

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-6-29
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1976-6696
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
350-5
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Enzymatic properties of the N- and C-terminal halves of human hexokinase II.
pubmed:affiliation
Division of Nuclear Medicine, Department of Diagnostic Radiology, Research Institute of Radiological Science, Yonsei University College of Medicine, Seoul 120-752, Korea.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't