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Prepublished online as a Blood First Edition Paper on August 8, 2002; DOI 10.1182/blood-2002-06-1851. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-06-1851v1 101/1/345    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by van Wijk, R. Articles by van Solinge, W. W. Search for Related Content PubMed PubMed Citation Articles by van Wijk, R. Articles by van Solinge, W. W. Related Collections Red Cells Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 January 2003, Vol. 101, No. 1, pp. 345-347 RED CELLS Brief report HK Utrecht: missense mutation in the active site of human hexokinase associated with hexokinase deficiency and severe nonspherocytic hemolytic anemia Richard van Wijk, Gert Rijksen, Eric G. Huizinga, Hendrik K. Nieuwenhuis, and Wouter W. van Solinge From the Department of Clinical Chemistry and the Department of Hematology, University Medical Center Utrecht; Department of Crystal & Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands. Hexokinase deficiency is a rare autosomal recessive disease with a clinical phenotype of severe hemolysis. We report a novel homozygous missense mutation in exon 15 (c.2039C>G, HK [hexokinase] Utrecht) of HK1, the gene that encodes red blood cell-specific hexokinase-R, in a patient previously diagnosed with hexokinase deficiency. The Thr680Ser substitution predicted by this mutation affects a highly conserved residue in the enzyme's active site that interacts with phosphate moieties of adenosine diphosphate, adenosine triphosphate (ATP), and inhibitor glucose-6-phosphate. We correlated the molecular data to the severe clinical phenotype of the patient by means of altered enzymatic properties of partially purified hexokinase from the patient, notably with respect to Mg2+-ATP binding. These kinetic properties contradict those obtained from a recombinant mutant brain hexokinase-I with the same Thr680Ser substitution. This contradiction thereby stresses the valuable contribution of studying patients with hexokinase deficiency to achieve a better understanding of hexokinase's key role in glycolysis. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Bonnefond, M. Vaxillaire, Y. Labrune, C. Lecoeur, J.-C. Chevre, N. Bouatia-Naji, S. Cauchi, B. Balkau, M. Marre, J. Tichet, et al. Genetic Variant in HK1 Is Associated With a Proanemic State and A1C but Not Other Glycemic Control-Related Traits Diabetes, November 1, 2009; 58(11): 2687 - 2697. [Abstract] [Full Text] [PDF] K. M.K. de Vooght, W. W. van Solinge, A. C. van Wesel, S. Kersting, and R. van Wijk First mutation in the red blood cell-specific promoter of hexokinase combined with a novel missense mutation causes hexokinase deficiency and mild chronic hemolysis Haematologica, September 1, 2009; 94(9): 1203 - 1210. [Abstract] [Full Text] [PDF] R. van Wijk and W. W. van Solinge The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis Blood, December 15, 2005; 106(13): 4034 - 4042. [Abstract] [Full Text] [PDF]

	Copyright © 2003 by American Society of Hematology         Online ISSN: 1528-0020