PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9762360-5	1998	The effect of glucose on translocation is mimicked by mannose which is also phosphorylated by glucokinase as well as by competitive inhibitors of glucokinase (mannoheptulose and 5-thioglucose) which are not phosphorylated.	Mannose	54-61	glucokinase	Homo sapiens	94-105	
10679232-5	2000	Mannose, but not the nonmetabolized hexoses, 3-O-methylglucose or 2-deoxyglucose, increases glucokinase protein content.	Mannose	0-7	glucokinase	Homo sapiens	92-103	
8679719-3	1996	Likewise, there were obvious discrepancies between the kinetics of glucose, mannose and fructose phosphorylation by B-cell glucokinase, e.g. in terms of maximal velocity, and the secretory and metabolic responses to these hexoses in intact islets.	Mannose	76-83	glucokinase	Homo sapiens	123-134	
9350059-1	1997	Human B-cell glucokinase displays sigmoidal kinetics towards D-glucose or D-mannose, but fails to do so towards D-fructose.	Mannose	74-83	glucokinase	Homo sapiens	13-24	
7742312-2	1995	Measurements of kcat/Km showed that glucokinase phosphorylated the sugars in the order glucose = mannose > deoxyglucose > fructose = glucosamine.	Mannose	97-104	glucokinase	Homo sapiens	36-47	
7742312-11	1995	The calculated interaction energies of glucokinase with glucose, mannose, deoxyglucose, and fructose agree very well with the measured values of kcat/Km, which indicates that these sugars are recognized by binding to the open conformation of glucokinase.	Mannose	65-72	glucokinase	Homo sapiens	39-50	
7742312-11	1995	The calculated interaction energies of glucokinase with glucose, mannose, deoxyglucose, and fructose agree very well with the measured values of kcat/Km, which indicates that these sugars are recognized by binding to the open conformation of glucokinase.	Mannose	65-72	glucokinase	Homo sapiens	242-253	
3207996-12	1988	Only glucose derivatives with a sufficiently bulky substituent in position C-2, such as the glucokinase substrates glucose and mannose and the inhibitors mannoheptulose, glucosamine, and N-acetylglucosamine, protected glucokinase against inhibition by alloxan by binding to the active site of the enzyme.	Mannose	127-134	glucokinase	Homo sapiens	92-103	
2210070-4	1990	CHX-induced inactivation of glucokinase was blocked by the presence of its substrates (glucose and mannose) and an inhibitor (N-acetylglucosamine), all of which also protected against the inhibitory effect of the drug on glucose-induced insulin secretion.	Mannose	99-106	glucokinase	Homo sapiens	28-39	
6289902-3	1982	The activity on mannose was due to a highly specific mannokinase (ATP:D-mannose 6-phosphotransferase, EC 2.7.1.7) which has been separated from the glucokinase by Ultrogel AcA 54 gel filtration chromatography.	Mannose	16-23	glucokinase	Homo sapiens	148-159	
6489350-2	1984	Hexokinase D ("glucokinase") displays positive cooperativity with mannose with the same h values (1.5-1.6) as with glucose but with higher K0.5 values (8 mM at pH 8.0 and 12 mM at pH 7.5).	Mannose	66-73	glucokinase	Homo sapiens	15-27	
13840-6	1977	The Km for glucose of pea-seed glucokinase was 70 muM and the Km for mannose was 0.5 mM.	Mannose	69-76	glucokinase	Homo sapiens	31-42	
20453072-4	2010	Glucokinase efficiently activates glucose and mannose but activates fructose only to a minor extent.	Mannose	46-53	glucokinase	Homo sapiens	0-11