Characterization of a novel type III alcohol dehydrogenase from Thermococcus barophilus Ch5.
Alcohols
/ metabolism
Aldehyde Oxidoreductases
/ genetics
Amino Acid Motifs
Amino Acid Sequence
Archaeal Proteins
/ genetics
Base Sequence
Cations
/ pharmacology
Circular Dichroism
Conserved Sequence
Genes, Archaeal
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Mutagenesis, Site-Directed
Phylogeny
Protein Denaturation
Recombinant Proteins
/ metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Thermococcales
/ enzymology
Thermococcus
/ enzymology
Alcohol dehydrogenase
Biochemical characteristics
Hyperthermophilic Archaea
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
28 Feb 2021
28 Feb 2021
Historique:
received:
12
09
2020
revised:
25
12
2020
accepted:
26
12
2020
pubmed:
12
1
2021
medline:
20
4
2021
entrez:
11
1
2021
Statut:
ppublish
Résumé
The genome of the hyperthermophilic and piezophilic euryarchaeaon Thermococcus barophilus Ch5 encodes three putative alcohol dehydrogenases (Tba ADHs). Herein, we characterized Tba ADH
Identifiants
pubmed: 33428959
pii: S0141-8130(20)35377-0
doi: 10.1016/j.ijbiomac.2020.12.197
pii:
doi:
Substances chimiques
Alcohols
0
Archaeal Proteins
0
Cations
0
Recombinant Proteins
0
formaldehyde dehydrogenase (glutathione)
EC 1.1.1.284
Aldehyde Oxidoreductases
EC 1.2.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
491-501Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest All authors declare that there is no conflict of interests regarding the publication of this paper.