PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16665142-7	1986	While the in vitro phosphorylation of PEPCase from illuminated maize leaves by an endogenous protein kinase resulted in a partial inactivation ( approximately 25%) of the enzyme when assayed at pH 7 and subsaturating levels of PEP, effector modulation by l-malate and glucose-6-phosphate was relatively unaffected.	Glucose-6-Phosphate	268-287	MLO-like protein 4	Zea mays	38-45	
21491491-4	2011	The allosteric binding sites for aspartate (an inhibitor) and glucose-6-phosphate (an activator) observed in the Escherichia coli and Zea mays phosphoenolpyruvate carboxylase structures, respectively, are not conserved in the C. perfringens structure.	Glucose-6-Phosphate	62-81	MLO-like protein 4	Zea mays	143-174	
12781768-7	2003	In the case of maize C4-PEPC, the putative binding site for an allosteric activator (glucose 6-phosphate) was also revealed.	Glucose-6-Phosphate	85-104	MLO-like protein 4	Zea mays	24-28	
11527579-2	2001	Allosteric activators such as D-glucose-6-phosphate and glycine increase the affinity of PEPC for its substrate PEP at pH 8.0 and pH 7.0.	Glucose-6-Phosphate	30-51	MLO-like protein 4	Zea mays	89-93	
9787461-7	1998	Glucose 6-phosphate and glycine had little effect on the root-form PEPC at pH 7.3; they caused two-fold activation of the C4-form PEPC.	Glucose-6-Phosphate	0-19	MLO-like protein 4	Zea mays	130-134	
9048897-0	1997	Desensitization to glucose 6-phosphate of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal 5"-phosphate.	Glucose-6-Phosphate	19-38	MLO-like protein 4	Zea mays	42-73	
16668606-4	1992	Based on these and related observations, we propose that the Calvin cycle supplies the C(4) mesophyll cell with (a) a putative signal (e.g. phosphorylated metabolite, amino acid) that interacts with the cytoplasmic protein synthesis event to effect the light activation of PEPC-PK and the concomitant phosphorylation of PEPC, and (b) high levels of known positive effectors (e.g. triose-phosphate, glucose-6-phosphate) that interact directly with the carboxylase.	Glucose-6-Phosphate	398-417	MLO-like protein 4	Zea mays	273-277	
16668606-4	1992	Based on these and related observations, we propose that the Calvin cycle supplies the C(4) mesophyll cell with (a) a putative signal (e.g. phosphorylated metabolite, amino acid) that interacts with the cytoplasmic protein synthesis event to effect the light activation of PEPC-PK and the concomitant phosphorylation of PEPC, and (b) high levels of known positive effectors (e.g. triose-phosphate, glucose-6-phosphate) that interact directly with the carboxylase.	Glucose-6-Phosphate	398-417	MLO-like protein 4	Zea mays	320-324	
32459324-1	2020	Activation of phosphoenolpyruvate carboxylase (PEPC) enzymes by glucose 6-phosphate (G6P) and other phospho-sugars is of major physiological relevance.	Glucose-6-Phosphate	85-88	MLO-like protein 4	Zea mays	14-45	
32459324-1	2020	Activation of phosphoenolpyruvate carboxylase (PEPC) enzymes by glucose 6-phosphate (G6P) and other phospho-sugars is of major physiological relevance.	Glucose-6-Phosphate	85-88	MLO-like protein 4	Zea mays	47-51	
23195383-9	1984	Moreover, the dissociation constants for phosphoenolpyruvate (plus or minus MgCl(2)) and malate in the presence of glucose-6-phosphate were calculated at pH 7.0, 7.5, and 7.9 from the protection afforded by these compounds against chemical modification of phosphoenolpyruvate carboxylase by phenylglyoxal.	Glucose-6-Phosphate	115-134	MLO-like protein 4	Zea mays	256-287