PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18553501-1	2008	In this article we report on the characterization of the enzymatic synthesis of D-xylulose 5-phosphate using triosephosphate isomerase and transketolase.	xylulose-5-phosphate	80-102	transketolase	Homo sapiens	139-152	
16732737-1	2006	Two new optical methods for transketolase activity assay using only one substrate, xylulose 5-phosphate or glycol aldehyde, have been developed.	xylulose-5-phosphate	83-103	transketolase	Homo sapiens	28-41	
18186462-1	2008	The effect of the type of the cation cofactor of transketolase (i.e., Ca2+ or Mg2+) on its interaction with xylulose 5-phosphate (donor substrate) has been studied.	xylulose-5-phosphate	108-128	transketolase	Homo sapiens	49-62	
18053578-1	2008	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.	xylulose-5-phosphate	80-102	transketolase	Homo sapiens	23-36	
17914867-2	2007	The X-ray structures of transketolase from E. coli in a covalent complex with donor ketoses d-xylulose 5-phosphate (X5P) and d-fructose 6-phosphate (F6P) at 1.47 A and 1.65 A resolution reveal significant strain in the tetrahedral cofactor-sugar adducts with a 25-30 degrees out-of-plane distortion of the C2-Calpha bond connecting the substrates" carbonyl with the C2 of the cofactor"s thiazolium part.	xylulose-5-phosphate	92-114	transketolase	Homo sapiens	24-37	
17914867-2	2007	The X-ray structures of transketolase from E. coli in a covalent complex with donor ketoses d-xylulose 5-phosphate (X5P) and d-fructose 6-phosphate (F6P) at 1.47 A and 1.65 A resolution reveal significant strain in the tetrahedral cofactor-sugar adducts with a 25-30 degrees out-of-plane distortion of the C2-Calpha bond connecting the substrates" carbonyl with the C2 of the cofactor"s thiazolium part.	xylulose-5-phosphate	116-119	transketolase	Homo sapiens	24-37	
6995116-1	1980	In the presence of hexacyanoferrate(III), or other suitable oxidants, transketolase catalyzes the oxidative cleavage of its donor substrates xylulose 5-phosphate or fructose 6-phosphate into glycolate and glyceraldehyde 3-phosphate or erythrose 4-phosphate, respectively.	xylulose-5-phosphate	141-161	transketolase	Homo sapiens	70-83	
11092965-2	2000	It is shown in this work that high concentrations of ribose-5-phosphate (acceptor substrate) compete with xylulose-5-phosphate (donor substrate), suppressing the transketolase activity (Ki = 3.8 mM).	xylulose-5-phosphate	106-126	transketolase	Homo sapiens	162-175	
11278369-1	2001	The cleavage of the donor substrate d-xylulose 5-phosphate by wild-type and H263A mutant yeast transketolase was studied using enzyme kinetics and circular dichroism spectroscopy.	xylulose-5-phosphate	36-58	transketolase	Homo sapiens	95-108	
11162599-1	2001	Apart from catalyzing the common two-substrate reaction with ketose as donor substrate and aldose as acceptor substrate, transketolase is also able to catalyze a one-substrate reaction utilizing only ketose (xylulose 5-phosphate) as substrate.	xylulose-5-phosphate	208-228	transketolase	Homo sapiens	121-134	
2495942-3	1989	The enzyme was finally detached from CM-cellulose by specific elution with a D-xylulose-5-phosphate/D-ribose-5-phosphate mixture and the isolated product exhibited a specific activity of about 10 units/mg protein at 37 degrees C. Transketolase preparations are contamination-free, except for a slight residual activity of phosphohexose isomerase.	xylulose-5-phosphate	77-99	transketolase	Homo sapiens	230-243	
5096513-5	1971	The specific effect on transketolase by uremic material was established by showing suppressed formation of S7P from R5P also in the presence of excess cofactor thiamine pyrophosphate and of the other substrate xylulose-5-phosphate.	xylulose-5-phosphate	210-230	transketolase	Homo sapiens	23-36