Title : Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A.

Pub. Date : 2007 Dec 14

PMID : 17956868






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Replacing Pro-40 of UGT1A4 by histidine expanded the glucuronidation activity of the enzyme to phenolic and carboxylic compounds, therefore, leading to UGT1A3-type isoform in terms of substrate specificity. Histidine UDP glucuronosyltransferase family 1 member A4 Homo sapiens
2 Conversely, when His-40 residue of UGT1A3 was replaced with proline, the substrate specificity shifted toward that of UGT1A4 with loss of glucuronidation of phenolic substrates. Histidine UDP glucuronosyltransferase family 1 member A4 Homo sapiens
3 Furthermore, mutation of His-39 residue of UGT1A1 (His-40 in UGT1A4) to proline led to loss of glucuronidation of phenols but not of estrogens. Histidine UDP glucuronosyltransferase family 1 member A4 Homo sapiens
4 Furthermore, mutation of His-39 residue of UGT1A1 (His-40 in UGT1A4) to proline led to loss of glucuronidation of phenols but not of estrogens. Histidine UDP glucuronosyltransferase family 1 member A4 Homo sapiens