Pub. Date : 1997 Oct
PMID : 9337154
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT. | Cysteine | methionine adenosyltransferase 1A | Homo sapiens |
2 | In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT. | Cysteine | methionine adenosyltransferase 1A | Homo sapiens |
3 | In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT. | Cysteine | methionine adenosyltransferase 1A | Homo sapiens |
4 | Cysteine 121 is specific to the hepatic enzyme and is localized at a "flexible loop" over the active site cleft of MAT. | Cysteine | methionine adenosyltransferase 1A | Homo sapiens |
5 | In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical. | Cysteine | methionine adenosyltransferase 1A | Homo sapiens |
6 | In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical. | Cysteine | methionine adenosyltransferase 1A | Homo sapiens |