PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	Glycine	23-30	OCA2 melanosomal transmembrane protein	Gallus gallus	59-68
6863283-2	1983	Chicken liver P-protein of the multienzyme glycine cleavage system catalyzes the first partial reaction of glycine cleavage.	Glycine	43-50	OCA2 melanosomal transmembrane protein	Gallus gallus	14-23
6863283-2	1983	Chicken liver P-protein of the multienzyme glycine cleavage system catalyzes the first partial reaction of glycine cleavage.	Glycine	107-114	OCA2 melanosomal transmembrane protein	Gallus gallus	14-23
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	Glycine	23-30	OCA2 melanosomal transmembrane protein	Gallus gallus	163-172
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	14co2	31-36	OCA2 melanosomal transmembrane protein	Gallus gallus	59-68
7440562-2	1980	Glycine decarboxylase, tentatively called P-protein and considered a constituent of the glycine cleavage system, was purified to apparent homogeneity from chicken liver mitochondria.	Glycine	88-95	OCA2 melanosomal transmembrane protein	Gallus gallus	42-51
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	14co2	31-36	OCA2 melanosomal transmembrane protein	Gallus gallus	163-172
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	tiglyl-coenzyme A	126-136	OCA2 melanosomal transmembrane protein	Gallus gallus	59-68
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	tiglyl-coenzyme A	126-136	OCA2 melanosomal transmembrane protein	Gallus gallus	163-172
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	tiglyl-coenzyme A	126-136	OCA2 melanosomal transmembrane protein	Gallus gallus	282-291
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	Cysteamine	245-255	OCA2 melanosomal transmembrane protein	Gallus gallus	59-68
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	Cysteamine	245-255	OCA2 melanosomal transmembrane protein	Gallus gallus	163-172
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	Glycine	336-343	OCA2 melanosomal transmembrane protein	Gallus gallus	59-68
6679320-3	1983	Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax.	Glycine	336-343	OCA2 melanosomal transmembrane protein	Gallus gallus	163-172
6815172-1	1982	The exchange of glycine carboxyl carbon with CO2 catalyzed by the combination of chicken liver glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) was markedly inhibited by various divalent cations, although extents of inhibition by individual metal ions varied considerably.	glycine carboxyl	16-32	OCA2 melanosomal transmembrane protein	Gallus gallus	118-127
6815172-1	1982	The exchange of glycine carboxyl carbon with CO2 catalyzed by the combination of chicken liver glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) was markedly inhibited by various divalent cations, although extents of inhibition by individual metal ions varied considerably.	Carbon	33-39	OCA2 melanosomal transmembrane protein	Gallus gallus	118-127
6815172-1	1982	The exchange of glycine carboxyl carbon with CO2 catalyzed by the combination of chicken liver glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) was markedly inhibited by various divalent cations, although extents of inhibition by individual metal ions varied considerably.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	45-48	OCA2 melanosomal transmembrane protein	Gallus gallus	118-127
6815172-1	1982	The exchange of glycine carboxyl carbon with CO2 catalyzed by the combination of chicken liver glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein) was markedly inhibited by various divalent cations, although extents of inhibition by individual metal ions varied considerably.	Metals	270-275	OCA2 melanosomal transmembrane protein	Gallus gallus	118-127
6815172-6	1982	The primary site of the action of divalent metal ions is likely to be not P-protein but H-protein, and the binding of metal ions with the H-protein-bound intermediate of glycine decarboxylation was assumed to account for the observed marked inhibition.	Metals	43-48	OCA2 melanosomal transmembrane protein	Gallus gallus	74-83
7440562-6	1980	P-protein could bind glycine, showing a Kd of 33 mM for it, and could catalyze glycine decarboxylation even though the rate of decarboxylation catalyzed by P-protein alone was extremely low.	Glycine	21-28	OCA2 melanosomal transmembrane protein	Gallus gallus	0-9
7440562-6	1980	P-protein could bind glycine, showing a Kd of 33 mM for it, and could catalyze glycine decarboxylation even though the rate of decarboxylation catalyzed by P-protein alone was extremely low.	Glycine	79-86	OCA2 melanosomal transmembrane protein	Gallus gallus	0-9
7440562-8	1980	Methylamine could bind to P-protein, giving a Kd value of 63 mM, and it inhibited the glycine decarboxylation.	methylamine	0-11	OCA2 melanosomal transmembrane protein	Gallus gallus	26-35
7440562-9	1980	P-protein alone could also slightly catalyze the exchange of carboxyl carbon of glycine with CO2 and the exchange appeared to obey a ping-pong mechanism.	Carbon	70-76	OCA2 melanosomal transmembrane protein	Gallus gallus	0-9
7440562-9	1980	P-protein alone could also slightly catalyze the exchange of carboxyl carbon of glycine with CO2 and the exchange appeared to obey a ping-pong mechanism.	Glycine	80-87	OCA2 melanosomal transmembrane protein	Gallus gallus	0-9
7440562-9	1980	P-protein alone could also slightly catalyze the exchange of carboxyl carbon of glycine with CO2 and the exchange appeared to obey a ping-pong mechanism.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	93-96	OCA2 melanosomal transmembrane protein	Gallus gallus	0-9
7440562-10	1980	Both glycine decarboxylation and the glycine-CO2 exchange catalyzed by P-protein were stimulated 100-fold or more by the addition of lipoic acid, which is a functional group of H-protein.	Glycine	5-12	OCA2 melanosomal transmembrane protein	Gallus gallus	71-80
7440562-10	1980	Both glycine decarboxylation and the glycine-CO2 exchange catalyzed by P-protein were stimulated 100-fold or more by the addition of lipoic acid, which is a functional group of H-protein.	Glycine	37-44	OCA2 melanosomal transmembrane protein	Gallus gallus	71-80
7440562-10	1980	Both glycine decarboxylation and the glycine-CO2 exchange catalyzed by P-protein were stimulated 100-fold or more by the addition of lipoic acid, which is a functional group of H-protein.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	45-48	OCA2 melanosomal transmembrane protein	Gallus gallus	71-80
7440562-10	1980	Both glycine decarboxylation and the glycine-CO2 exchange catalyzed by P-protein were stimulated 100-fold or more by the addition of lipoic acid, which is a functional group of H-protein.	Thioctic Acid	133-144	OCA2 melanosomal transmembrane protein	Gallus gallus	71-80
3426593-0	1987	Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system.	phosphopyridoxyl peptide	27-51	OCA2 melanosomal transmembrane protein	Gallus gallus	57-66
3426593-0	1987	Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system.	Glycine	88-95	OCA2 melanosomal transmembrane protein	Gallus gallus	57-66
3426593-1	1987	A pyridoxal 5"-phosphate-containing peptide which contained 54 amino acid residues was isolated from chicken liver P-protein of the glycine cleavage system following reduction with NaB3H4, carboxymethylation, and proteolysis with lysylendopeptidase.	Pyridoxal Phosphate	2-24	OCA2 melanosomal transmembrane protein	Gallus gallus	115-124
3426593-1	1987	A pyridoxal 5"-phosphate-containing peptide which contained 54 amino acid residues was isolated from chicken liver P-protein of the glycine cleavage system following reduction with NaB3H4, carboxymethylation, and proteolysis with lysylendopeptidase.	Glycine	132-139	OCA2 melanosomal transmembrane protein	Gallus gallus	115-124
3426593-1	1987	A pyridoxal 5"-phosphate-containing peptide which contained 54 amino acid residues was isolated from chicken liver P-protein of the glycine cleavage system following reduction with NaB3H4, carboxymethylation, and proteolysis with lysylendopeptidase.	nab3h4	181-187	OCA2 melanosomal transmembrane protein	Gallus gallus	115-124