Molecular basis of hyper-thermostability in the thermophilic archaeal aldolase MfnB.
Aldolase
Methanofuran
Methanogenesis
Protein folding
Thermostability
Journal
Extremophiles : life under extreme conditions
ISSN: 1433-4909
Titre abrégé: Extremophiles
Pays: Germany
ID NLM: 9706854
Informations de publication
Date de publication:
31 Aug 2024
31 Aug 2024
Historique:
received:
08
05
2024
accepted:
20
08
2024
medline:
1
9
2024
pubmed:
1
9
2024
entrez:
31
8
2024
Statut:
epublish
Résumé
Methanogenic archaea are chemolithotrophic prokaryotes that can reduce carbon dioxide with hydrogen gas to form methane. These microorganisms make a significant contribution to the global carbon cycle, with methanogenic archaea from anoxic environments estimated to contribute > 500 million tons of global methane annually. Archaeal methanogenesis is dependent on the methanofurans; aminomethylfuran containing coenzymes that act as the primary C
Identifiants
pubmed: 39215799
doi: 10.1007/s00792-024-01359-x
pii: 10.1007/s00792-024-01359-x
doi:
Substances chimiques
Archaeal Proteins
0
Aldehyde-Lyases
EC 4.1.2.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
42Subventions
Organisme : Engineering and Physical Sciences Research Council
ID : EP/L016494/1
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L01386X/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M025624/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/T001968/1
Pays : United Kingdom
Organisme : Defence Science and Technology Laboratory
ID : DSTLX1000098188
Organisme : Defence Science and Technology Laboratory
ID : DSTLX1000133108
Informations de copyright
© 2024. The Author(s).
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