Biochemical characterization and mutational analysis of alanine racemase from Clostridium perfringens.
Alanine racemase
Clostridium perfringens
Dimer interface
Entryway corridor
Site-directed mutagenesis
Journal
Journal of bioscience and bioengineering
ISSN: 1347-4421
Titre abrégé: J Biosci Bioeng
Pays: Japan
ID NLM: 100888800
Informations de publication
Date de publication:
Aug 2019
Aug 2019
Historique:
received:
17
11
2018
revised:
03
02
2019
accepted:
06
02
2019
pubmed:
4
3
2019
medline:
12
10
2019
entrez:
4
3
2019
Statut:
ppublish
Résumé
Clostridium perfringens is a gram-positive, anaerobic, pathogenic bacterium that can cause a wide range of diseases in humans, poultry and agriculturally important livestock. A pyridoxal-5-phosphate-dependent alanine racemase with a function in the racemization of d- and l-alanine is an attractive drug target for C. perfringens and other pathogens due to its absence in animals and humans. In this study alanine racemase from C. perfringens (CPAlr) was successfully expressed and purified in Escherichia coli and biochemically characterized. The purified CPAlr protein was a dimeric PLP-dependent enzyme with high substrate specificity. The optimal racemization temperature and pH were 40°C and 8.0, respectively. The kinetic parameters K
Identifiants
pubmed: 30826314
pii: S1389-1723(18)31039-9
doi: 10.1016/j.jbiosc.2019.02.003
pii:
doi:
Substances chimiques
Pyridoxal Phosphate
5V5IOJ8338
Alanine Racemase
EC 5.1.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
149-155Informations de copyright
Copyright © 2019 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.