[PDF][PDF] Stereochemical and steric control of enzymatic glucuronidation: A rational approach for the design of novel Inhibitors for the human UDP …

I Bichlmaier - 2008 - core.ac.uk
The UDP-glucuronosyltransferases (UGTs) are enzymes of the phase II metabolic system.
These enzymes catalyze the transfer of α-D-glucuronic acid from UDP-glucuronic acid to …

1H, 13C, 15N Backbone and sidechain chemical shift assignments of the C-terminal domain of human UDP-glucuronosyltransferase 2B17 (UGT2B17-C)

A Sulekha, MJ Osborne, J Gasiorek… - Biomolecular NMR …, 2023 - Springer
UDP-glucuronosyltransferases are the principal enzymes involved in the glucuronidation of
metabolites and xenobiotics for physiological clearance in humans. Though glucuronidation …

A broad-spectrum substrate for the human UDP-glucuronosyltransferases and its use for investigating glucuronidation inhibitors

QH Zhou, WW Qin, M Finel, QQ He, DZ Tu… - International Journal of …, 2021 - Elsevier
Strong inhibition of the human UDP-glucuronosyltransferase enzymes (UGTs) may lead to
undesirable effects, including hyperbilirubinaemia and drug/herb-drug interactions …

Glucuronidation activity of individual UDP-glucuronosyltransferases: Comparison of activity and substrate specificity among recombinant human UGT enzymes and …

J Troberg - 2019 - helda.helsinki.fi
UDP-glucuronosyltransferases (UGTs) are a group of important conjugation enzymes that
transfer a sugar moiety from UDP-glucuronic acid onto a nucleophilic group in substrate …

Natural and synthetic inhibitors of UDP-glucuronosyltransferase

K Grancharov, Z Naydenova, S Lozeva… - Pharmacology & …, 2001 - Elsevier
Glucuronidation is a major detoxification pathway in vertebrates. The reaction is catalyzed
by a family of UDP-glucuronosyltransferases (UGTs) and involves conjugation of many …

Effects of amino acid substitutions at positions 33 and 37 on UDP-glucuronosyltransferase 1A9 (UGT1A9) activity and substrate selectivity

P Korprasertthaworn, A Rowland, BC Lewis… - Biochemical …, 2012 - Elsevier
UGT1A9 contributes to the glucuronidation of numerous drugs and xenobiotics. There is
evidence to suggest that the Met33Thr substitution, as occurs in the polymorphic variant …

Molecular docking-based design and development of a highly selective probe substrate for UDP-glucuronosyltransferase 1A10

RO Juvonen, S Rauhamäki, S Kortet… - Molecular …, 2018 - ACS Publications
Intestinal and hepatic glucuronidation by the UDP-glucuronosyltransferases (UGTs) greatly
affect the bioavailability of phenolic compounds. UGT1A10 catalyzes glucuronidation …

How many and which amino acids are responsible for the large activity differences between the highly homologous UDP-glucuronosyltransferases (UGT) 1A9 and …

K Itäaho, L Laakkonen, M Finel - Drug metabolism and disposition, 2010 - ASPET
The amino acid sequences of the human UDP-glucuronosyltransferases (UGTs) 1A9 and
1A10 are 93% identical, yet there are large differences in their activity and substrate …

Human UDP-glucuronosyltransferase (UGT) 2B10 in drug N-glucuronidation: substrate screening and comparison with UGT1A3 and UGT1A4

Y Kato, T Izukawa, S Oda, T Fukami, M Finel… - Drug Metabolism and …, 2013 - ASPET
Recent observations revealed that human UDP-glucuronosyltransferase (UGT) 2B10
catalyzes N-glucuronidation of amine-containing compounds. Knowledge of the substrate …

Stereochemical and Steric Control of the UDP‐Glucuronosyltransferase‐Catalyzed Conjugation Reaction: A Rational Approach for the Design of Inhibitors for the …

I Bichlmaier, M Finel, W Sippl… - ChemMedChem …, 2007 - Wiley Online Library
A set of 76 derivatives of the epimeric tricyclic sesquiterpenols longifolol and isolongifolol
was subjected to inhibition and glucuronidation assays employing the human UDP …