Structural and functional analyses of a novel manganese-catalase from Bacillus subtilis R5.
Bacillus subtilis
/ enzymology
Bacterial Proteins
/ chemistry
Calcium
/ metabolism
Catalase
/ chemistry
Catalytic Domain
Cloning, Molecular
/ methods
Escherichia coli
/ genetics
Half-Life
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Manganese
/ metabolism
Molecular Docking Simulation
Molecular Weight
Phylogeny
Protein Binding
Solubility
Bacillus subtilis
Hydrogen peroxide
Manganese-catalase
Metalloenzyme
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:
01 Jun 2021
01 Jun 2021
Historique:
received:
16
01
2021
revised:
13
03
2021
accepted:
13
03
2021
pubmed:
20
3
2021
medline:
27
7
2021
entrez:
19
3
2021
Statut:
ppublish
Résumé
Catalases catalyze the decomposition of hydrogen peroxide into water and oxygen. Limited reports are available on characterization of manganese-catalases. We describe here molecular cloning and expression in Escherichia coli of a putative manganese-catalase gene from mesophilic bacterium, Bacillus subtilis R5. The gene product, Cat
Identifiants
pubmed: 33737179
pii: S0141-8130(21)00592-4
doi: 10.1016/j.ijbiomac.2021.03.074
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Manganese
42Z2K6ZL8P
Catalase
EC 1.11.1.6
Calcium
SY7Q814VUP
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
222-233Informations de copyright
Copyright © 2021. Published by Elsevier B.V.