Characterization of enzymatic D-xylulose 5-phosphate synthesis.
In this article we report on the characterization of the enzymatic synthesis of D-xylulose 5-phosphate using triosephosphate isomerase and transketolase. Two potential starting substrates are possible with this scheme. The data presented here allow a comparison of both routes for the synthesis, based on experimental information on reaction kinetics. Operational guidelines are proposed which should assist in the scale-up of such syntheses.
Shaeri
Jobin
J
Department of Biochemical Engineering, University College London, Torrington Place, London, UK.
Wright
Ian
I
Rathbone
Elner B
EB
Wohlgemuth
Roland
R
Woodley
John M
JM
D004099:Dihydroxyacetone Phosphate / Q000378:metabolism; D004795:Enzyme Stability; D005986:Glyceraldehyde 3-Phosphate / Q000378:metabolism; D007700:Kinetics; D010428:Pentosephosphates / Q000096:biosynthesis*; D014174:Transketolase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D014305:Triose-Phosphate Isomerase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D010428:Pentosephosphates; D005986:Glyceraldehyde 3-Phosphate; D004099:Dihydroxyacetone Phosphate; C031625:xylulose-5-phosphate; D014174:Transketolase; D014305:Triose-Phosphate Isomerase