Reconstitution of holotransketolase is by a thiamin-disphosphate-magnesium complex

Booth, CK and Nixon, PF (1993) Reconstitution of holotransketolase is by a thiamin-disphosphate-magnesium complex. European Journal of Biochemistry, 218 1: 261-265. doi:10.1111/j.1432-1033.1993.tb18373.x

Author Booth, CK
Nixon, PF
Title Reconstitution of holotransketolase is by a thiamin-disphosphate-magnesium complex
Journal name European Journal of Biochemistry   Check publisher's open access policy
ISSN 0014-2956
Publication date 1993-01-01
Year available 1993
Sub-type Article (original research)
DOI 10.1111/j.1432-1033.1993.tb18373.x
Open Access Status Not yet assessed
Volume 218
Issue 1
Start page 261
End page 265
Total pages 5
Place of publication NEW YORK
Language eng
Subject 1303 Specialist Studies in Education
Abstract When human erythrocyte apo-transketolase is mixed with cofactors and substrates, the progress curve exhibits a lag phase. Elimination of the lag phase requires the presence of saturating concentrations of cofactors, thiamin diphosphate and Mg2+. The most simple explanation of the observed hysteretic transition is that the slow binding of a Mg2+-thiamin-diphosphate species precedes slow isomerisation of the enzyme to the active form. Although the hysteretic transition involves more than one process, it does not involve the dissociation-association of enzyme subunits. The best estimate of the apparent K(m), 1.59 +/- 0.23 muM, for the binding of Mg2+-thiamin diphosphate to transketolase was obtained in the presence of a high non-inhibitory concentration of magnesium and varied concentrations of thiamin diphosphate. Thus the reconstitution of the human enzyme differs from the yeast enzyme, which undergoes a rate-limiting dimerisation during reconstitution.
Keyword Biochemistry & Molecular Biology
Biochemistry & Molecular Biology
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 12 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 11 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sat, 12 Sep 2015, 04:37:28 EST by System User