Pub. Date : 2003 Sep 12
PMID : 12842883
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Molecular dissection of the S-adenosylmethionine-binding site of phosphatidylethanolamine N-methyltransferase. | S-Adenosylmethionine | phosphatidylethanolamine N-methyltransferase | Homo sapiens |
| 2 | To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). | S-Adenosylmethionine | phosphatidylethanolamine N-methyltransferase | Homo sapiens |
| 3 | To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). | S-Adenosylmethionine | phosphatidylethanolamine N-methyltransferase | Homo sapiens |
| 4 | To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). | S-Adenosylmethionine | phosphatidylethanolamine N-methyltransferase | Homo sapiens |
| 5 | To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). | S-Adenosylmethionine | phosphatidylethanolamine N-methyltransferase | Homo sapiens |