Pub. Date : 2020 Dec
PMID : 33008919
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Although UDP-glucuronic acid (UDP-GlcUA) is most commonly employed as the cofactor by UGT1 and UGT2 family enzymes, UGT2B7 and several other enzymes can utilise both UDP-GlcUA and UDP-glucose (UDP-Glc), leading to the formation of glucuronide and glucoside conjugates. | Uridine Diphosphate Glucuronic Acid | UDP glucuronosyltransferase family 2 member B7 | Homo sapiens |
| 2 | Although UDP-glucuronic acid (UDP-GlcUA) is most commonly employed as the cofactor by UGT1 and UGT2 family enzymes, UGT2B7 and several other enzymes can utilise both UDP-GlcUA and UDP-glucose (UDP-Glc), leading to the formation of glucuronide and glucoside conjugates. | Uridine Diphosphate Glucuronic Acid | UDP glucuronosyltransferase family 2 member B7 | Homo sapiens |
| 3 | Although UDP-glucuronic acid (UDP-GlcUA) is most commonly employed as the cofactor by UGT1 and UGT2 family enzymes, UGT2B7 and several other enzymes can utilise both UDP-GlcUA and UDP-glucose (UDP-Glc), leading to the formation of glucuronide and glucoside conjugates. | Uridine Diphosphate Glucuronic Acid | UDP glucuronosyltransferase family 2 member B7 | Homo sapiens |
| 4 | An investigation of UGT2B7 catalysed morphine glycosidation indicated that glucuronidation is the principal route of metabolism because the binding affinity of UDP-GlcUA is higher than that of UDP-Glc. | Uridine Diphosphate Glucuronic Acid | UDP glucuronosyltransferase family 2 member B7 | Homo sapiens |
| 5 | Currently, it is unclear which residues in the UGT2B7 cofactor binding domain are responsible for the preferential binding of UDP-GlcUA. | Uridine Diphosphate Glucuronic Acid | UDP glucuronosyltransferase family 2 member B7 | Homo sapiens |