PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
21320452-6	2011	We find that 1), a distortion of Glu(183) is important for CPO-catalyzed epoxidation as was postulated previously based on experimental results; 2), the free energy of binding does not provide significant differentiation between structures leading to the respective epoxide enantiomers; and 3), CPO"s enantiospecificity toward cis-beta-methylstyrene is likely to be caused by a specific group of residues which form a hydrophobic core surrounding the oxyferryl heme center.	Glutamic Acid	33-36	carboxypeptidase O	Homo sapiens	59-62
21921028-5	2011	CPO was purified by affinity chromatography, and the purified enzyme was able to cleave proteins and synthetic peptides with greatest activity toward acidic C-terminal amino acids unlike other CPA-like enzymes.	Peptides	111-119	carboxypeptidase O	Homo sapiens	0-3
21921028-6	2011	CPO displayed a neutral pH optimum and was inhibited by common metallocarboxypeptidase inhibitors as well as citrate.	Citric Acid	109-116	carboxypeptidase O	Homo sapiens	0-3
21921028-7	2011	CPO was modified by attachment of a glycosylphosphatidylinositol membrane anchor to the C terminus of the protein.	Glycosylphosphatidylinositols	36-64	carboxypeptidase O	Homo sapiens	0-3
21921028-10	2011	These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB.	Acids	39-45	carboxypeptidase O	Homo sapiens	27-30
21921028-10	2011	These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB.	cpb	175-178	carboxypeptidase O	Homo sapiens	27-30
30921734-3	2019	Here, we utilize GOx-CPO as integrated tandem enzymes to in situ generate singlet oxygen, which could be not only for oxidative cross-linking of injectable hydrogel carriers but also for continuous tumor treatment by adjustable bioconversion of blood oxygen, glucose, and chloride ion.	Singlet Oxygen	74-88	carboxypeptidase O	Homo sapiens	21-24
30921734-3	2019	Here, we utilize GOx-CPO as integrated tandem enzymes to in situ generate singlet oxygen, which could be not only for oxidative cross-linking of injectable hydrogel carriers but also for continuous tumor treatment by adjustable bioconversion of blood oxygen, glucose, and chloride ion.	Oxygen	82-88	carboxypeptidase O	Homo sapiens	21-24
30921734-3	2019	Here, we utilize GOx-CPO as integrated tandem enzymes to in situ generate singlet oxygen, which could be not only for oxidative cross-linking of injectable hydrogel carriers but also for continuous tumor treatment by adjustable bioconversion of blood oxygen, glucose, and chloride ion.	Glucose	259-266	carboxypeptidase O	Homo sapiens	21-24
30921734-3	2019	Here, we utilize GOx-CPO as integrated tandem enzymes to in situ generate singlet oxygen, which could be not only for oxidative cross-linking of injectable hydrogel carriers but also for continuous tumor treatment by adjustable bioconversion of blood oxygen, glucose, and chloride ion.	Chlorides	272-280	carboxypeptidase O	Homo sapiens	21-24
29636417-4	2018	This residue, located at "canonical" position 255, where it is Ile in human pancreatic carboxypeptidases A1 (hCPA1) and A2 (hCPA2) and Asp in B (hCPB), plays a dominant role in determining the preference of hCPO for acidic C-t residues.	Isoleucine	63-66	carboxypeptidase O	Homo sapiens	207-211
29636417-4	2018	This residue, located at "canonical" position 255, where it is Ile in human pancreatic carboxypeptidases A1 (hCPA1) and A2 (hCPA2) and Asp in B (hCPB), plays a dominant role in determining the preference of hCPO for acidic C-t residues.	Aspartic Acid	135-138	carboxypeptidase O	Homo sapiens	207-211
29636417-7	2018	hCPO also shows a preference for Glu over Asp, probably as a consequence of a tighter fitting of the Glu side chain in its S1" substrate-binding pocket.	Glutamic Acid	33-36	carboxypeptidase O	Homo sapiens	0-4
29636417-7	2018	hCPO also shows a preference for Glu over Asp, probably as a consequence of a tighter fitting of the Glu side chain in its S1" substrate-binding pocket.	Aspartic Acid	42-45	carboxypeptidase O	Homo sapiens	0-4
29636417-7	2018	hCPO also shows a preference for Glu over Asp, probably as a consequence of a tighter fitting of the Glu side chain in its S1" substrate-binding pocket.	Glutamic Acid	101-104	carboxypeptidase O	Homo sapiens	0-4
23639873-4	2013	CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated.	Threonine	75-85	carboxypeptidase O	Homo sapiens	0-4
21320452-6	2011	We find that 1), a distortion of Glu(183) is important for CPO-catalyzed epoxidation as was postulated previously based on experimental results; 2), the free energy of binding does not provide significant differentiation between structures leading to the respective epoxide enantiomers; and 3), CPO"s enantiospecificity toward cis-beta-methylstyrene is likely to be caused by a specific group of residues which form a hydrophobic core surrounding the oxyferryl heme center.	Glutamic Acid	33-36	carboxypeptidase O	Homo sapiens	295-298
21320452-6	2011	We find that 1), a distortion of Glu(183) is important for CPO-catalyzed epoxidation as was postulated previously based on experimental results; 2), the free energy of binding does not provide significant differentiation between structures leading to the respective epoxide enantiomers; and 3), CPO"s enantiospecificity toward cis-beta-methylstyrene is likely to be caused by a specific group of residues which form a hydrophobic core surrounding the oxyferryl heme center.	cis-Propenylbenzene	327-349	carboxypeptidase O	Homo sapiens	59-62
21320452-6	2011	We find that 1), a distortion of Glu(183) is important for CPO-catalyzed epoxidation as was postulated previously based on experimental results; 2), the free energy of binding does not provide significant differentiation between structures leading to the respective epoxide enantiomers; and 3), CPO"s enantiospecificity toward cis-beta-methylstyrene is likely to be caused by a specific group of residues which form a hydrophobic core surrounding the oxyferryl heme center.	oxyferryl heme	451-465	carboxypeptidase O	Homo sapiens	59-62
26631697-6	2008	We find that nom-CPO level captures the bulk of the static correlation energy, and MRMP2/nom-CPO calculations have an average error of only 1.4 kcal/mol in barrier heights, which may be compared to 5.0 kcal/mol for single-reference MP2 theory, 2.5 kcal/mol for CCSD, and 4.1 and 1.0 kcal/mol for the B3LYP and M06-2X density functionals, respectively.	ccsd	261-265	carboxypeptidase O	Homo sapiens	93-96
11250567-5	2001	The Sn--O distances for O atoms trans to carboxylate groups are shorter than those trans to phosphonate groups and d(Sn--O) decreases with increasing d(C/P--O) (Delta(Sn--O) approximately -4.6 Delta(C/P--O)).	carboxylate	41-52	carboxypeptidase O	Homo sapiens	154-206
11250567-5	2001	The Sn--O distances for O atoms trans to carboxylate groups are shorter than those trans to phosphonate groups and d(Sn--O) decreases with increasing d(C/P--O) (Delta(Sn--O) approximately -4.6 Delta(C/P--O)).	Organophosphonates	92-103	carboxypeptidase O	Homo sapiens	154-206