The metal cofactor: stationary or mobile?
Class II aldolase
Medium-chain dehydrogenase
Metal cofactor
Metal movement
Xylose isomerase
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
24 Jun 2024
24 Jun 2024
Historique:
received:
11
03
2024
accepted:
27
05
2024
revised:
22
05
2024
medline:
24
6
2024
pubmed:
24
6
2024
entrez:
23
6
2024
Statut:
epublish
Résumé
Metal cofactors are essential for catalysis and enable countless conversions in nature. Interestingly, the metal cofactor is not always static but mobile with movements of more than 4 Å. These movements of the metal can have different functions. In the case of the xylose isomerase and medium-chain dehydrogenases, it clearly serves a catalytic purpose. The metal cofactor moves during substrate activation and even during the catalytic turnover. On the other hand, in class II aldolases, the enzymes display resting states and active states depending on the movement of the catalytic metal cofactor. This movement is caused by substrate docking, causing the metal cofactor to take the position essential for catalysis. As these metal movements are found in structurally and mechanistically unrelated enzymes, it has to be expected that this metal movement is more common than currently perceived. KEY POINTS: • Metal ions are essential cofactors that can move during catalysis. • In class II aldolases, the metal cofactors can reside in a resting state and an active state. • In MDR, the movement of the metal cofactor is essential for substrate docking.
Identifiants
pubmed: 38910188
doi: 10.1007/s00253-024-13206-2
pii: 10.1007/s00253-024-13206-2
doi:
Substances chimiques
Metals
0
Coenzymes
0
Aldose-Ketose Isomerases
EC 5.3.1.-
xylose isomerase
EC 5.3.1.5
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
391Informations de copyright
© 2024. The Author(s).
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