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A new erythrose 4-phosphate dehydrogenase coupled assay for transketolase
- Source :
-
Journal of Proteomics . Apr2008, Vol. 70 Issue 6, p1185-1187. 3p. - Publication Year :
- 2008
-
Abstract
- Abstract: The standard assay for transketolase (E.C 2.2.1.1) has depended upon the use of d-xylulose 5-phosphate as the ketose donor substrate since the production of d-glyceraldehyde 3-phosphate can be readily coupled to a reaction that consumes NADH allowing the reaction to be followed spectrophotometrically. Unfortunately, commercial supplies of d-xylulose 5-phosphate recently became unavailable. In this article we describe the coupling of a transketolase reaction (using Leishmania mexicana transketolase) that converts d-fructose 6-phosphate to d-erythrose 4-phosphate. d-Erythrose 4-phosphate can then be converted to 4-phosphate d-erythronate using erythrose-4-phosphate dehydrogenase (E.C 1.2.1.72), a reaction that reduces NAD+ to NADH and can be easily followed spectrophotometrically. d-Ribose 5-phosphate and d-glyceraldehyde 3-phosphate can both be used as ketol acceptor substrates in the reaction although d-ribose 5-phosphate is also a substrate for the coupling enzyme. [Copyright &y& Elsevier]
- Subjects :
- *TRANSKETOLASE
*DEHYDROGENASES
*GLYCOSIDES
*ENZYMES
Subjects
Details
- Language :
- English
- ISSN :
- 18743919
- Volume :
- 70
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Journal of Proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 31751016
- Full Text :
- https://doi.org/10.1016/j.jprot.2007.11.002