One Key and Multiple Locks: Substrate Binding in Structures of Tryptophan Dioxygenases and Hydroxylases.
IDO
Molecular Recognition
TDO
TPH
Tryptophan
Journal
ChemMedChem
ISSN: 1860-7187
Titre abrégé: ChemMedChem
Pays: Germany
ID NLM: 101259013
Informations de publication
Date de publication:
16 09 2021
16 09 2021
Historique:
revised:
14
06
2021
received:
05
06
2021
pubmed:
18
6
2021
medline:
17
2
2022
entrez:
17
6
2021
Statut:
ppublish
Résumé
Since its discovery at the beginning of the past century, the essential nutrient l-Tryptophan (l-Trp) and its catabolic pathways have acquired an increasing interest in an ever wider scientific community for their pivotal roles in underlying many important physiological functions and associated pathological conditions. As a consequence, enzymes catalyzing rate limiting steps along l-Trp catabolic pathways - including IDO1, TDO, TPH1 and TPH2 - have turned to be interesting drug targets for the design and development of novel therapeutic agents for different disorders such as carcinoid syndrome, cancer and autoimmune diseases. This article provides a fresh comparative overview on the most recent advancements that crystallographic studies, biophysical and computational works have brought on structural aspects and molecular recognition patterns of these enzymes toward l-Trp. Finally, a conformational analysis of l-Trp is also discussed as part of the molecular recognition process governing the binding of a substrate to its cognate enzymes.
Identifiants
pubmed: 34137184
doi: 10.1002/cmdc.202100312
pmc: PMC8518741
doi:
Substances chimiques
Enzyme Inhibitors
0
IDO1 protein, human
0
Indoleamine-Pyrrole 2,3,-Dioxygenase
0
Tryptophan Oxygenase
EC 1.13.11.11
TPH1 protein, human
EC 1.14.16.4
TPH2 protein, human
EC 1.14.16.4
Tryptophan Hydroxylase
EC 1.14.16.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2732-2743Subventions
Organisme : University of Perugia (Ricerca di base 2020)
Informations de copyright
© 2021 The Authors. ChemMedChem published by Wiley-VCH GmbH.
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