Structure, Oligomerization and Activity Modulation in N-Ribohydrolases.
N-ribohydrolases
drug design
quaternary structure
ribosides
structural enzymology
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
25 Feb 2022
25 Feb 2022
Historique:
received:
05
01
2022
revised:
18
02
2022
accepted:
22
02
2022
entrez:
10
3
2022
pubmed:
11
3
2022
medline:
9
4
2022
Statut:
epublish
Résumé
Enzymes catalyzing the hydrolysis of the N-glycosidic bond in nucleosides and other ribosides (N-ribohydrolases, NHs) with diverse substrate specificities are found in all kingdoms of life. While the overall NH fold is highly conserved, limited substitutions and insertions can account for differences in substrate selection, catalytic efficiency, and distinct structural features. The NH structural module is also employed in monomeric proteins devoid of enzymatic activity with different physiological roles. The homo-oligomeric quaternary structure of active NHs parallels the different catalytic strategies used by each isozyme, while providing a buttressing effect to maintain the active site geometry and allow the conformational changes required for catalysis. The unique features of the NH catalytic strategy and structure make these proteins attractive targets for diverse therapeutic goals in different diseases.
Identifiants
pubmed: 35269719
pii: ijms23052576
doi: 10.3390/ijms23052576
pmc: PMC8910321
pii:
doi:
Substances chimiques
Nucleosides
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
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