Title : Interaction of liver methionine adenosyltransferase with hydroxyl radical.

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