Structure, mechanism and inhibition of anthranilate phosphoribosyltransferase.
AnPRT
PRT
TrpD
tryptophan biosynthesis
Journal
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
ISSN: 1471-2970
Titre abrégé: Philos Trans R Soc Lond B Biol Sci
Pays: England
ID NLM: 7503623
Informations de publication
Date de publication:
27 02 2023
27 02 2023
Historique:
entrez:
12
1
2023
pubmed:
13
1
2023
medline:
14
1
2023
Statut:
ppublish
Résumé
Anthranilate phosphoribosyltransferase catalyses the second reaction in the biosynthesis of tryptophan from chorismate in microorganisms and plants. The enzyme is homodimeric with the active site located in the hinge region between two domains. A range of structures in complex with the substrates, substrate analogues and inhibitors have been determined, and these have provided insights into the catalytic mechanism of this enzyme. Substrate 5-phospho-d-ribose 1-diphosphate (PRPP) binds to the C-terminal domain and coordinates to Mg
Identifiants
pubmed: 36633281
doi: 10.1098/rstb.2022.0039
pmc: PMC9835598
doi:
Substances chimiques
Anthranilate Phosphoribosyltransferase
EC 2.4.2.18
ortho-Aminobenzoates
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
20220039Références
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