PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2633802-0	1989	[Kinetic properties of transketolase from the rat liver in a reaction with xylulose-5-phosphate and ribose-5-phosphate].	xylulose-5-phosphate	75-95	transketolase	Rattus norvegicus	23-36	
6862092-11	1983	The coupled transketolase-transaldolase reactions, 2 fructose 6-phosphate in equilibrium altro-heptulose 7-phosphate + xylulose 5-phosphate and 2 altro-heptulose 7-phosphate in equilibrium fructose 6-phosphate + D-glycero D-altro octulose 8-phosphate were demonstrated with purified enzymes, but are concluded to play a minor role in the non-oxidative synthesis of pentose 5-phosphate and octulose phosphate by (RLEP).	xylulose-5-phosphate	119-139	transketolase	Rattus norvegicus	12-25	
7317524-5	1981	The curve for the reaction rate versus substrate concentration is S-shaped; the apparent Km value for xylulose 5-phosphate is 2.2 x 10(-5) M. The ions with a tetraedric structure (arsenate, phosphate, sulfate) act as competitive inhibitors of the transketolase-catalyzed reaction.	xylulose-5-phosphate	102-122	transketolase	Rattus norvegicus	247-260	
10080-7	1976	For the transketolase substrates, ribose 5-phosphate and xylulose 5-phosphate, the apparent Km values were 0.3 and 0.5 mM, respectively, in both liver and hepatoma.	xylulose-5-phosphate	57-77	transketolase	Rattus norvegicus	8-21	
7423874-1	1980	Inhibition of rat liver transketolase under conditions of hydroxythiamin or alimentary B1 avitaminosis was accompanied by an increase in intracellular concentration of 6-phosphogluconate and xylulose-5-phosphate.	xylulose-5-phosphate	191-211	transketolase	Rattus norvegicus	24-37