Pub. Date : 2011 Feb 16
PMID : 21320452
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | 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 | carboxypeptidase O | Homo sapiens |
| 2 | 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 | carboxypeptidase O | Homo sapiens |
| 3 | 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 | carboxypeptidase O | Homo sapiens |
| 4 | 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 | carboxypeptidase O | Homo sapiens |