Enzymatic properties and physiological function of glutamate racemase from Thermus thermophilus.
Amino Acid Isomerases
/ chemistry
Amino Acid Sequence
Amino Acids
/ metabolism
Cell Wall
/ chemistry
Cloning, Molecular
Enzyme Stability
Escherichia coli
/ metabolism
Gene Deletion
Genome, Bacterial
Glutamic Acid
/ metabolism
Hydrogen-Ion Concentration
Kinetics
Recombinant Proteins
Substrate Specificity
Temperature
Thermus thermophilus
/ enzymology
Transcriptome
Amino acid racemase
Glutamate racemase
Peptidoglycan
Thermus thermophilus
d-amino acid
d-glutamate
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
received:
25
02
2020
revised:
08
05
2020
accepted:
26
05
2020
pubmed:
1
6
2020
medline:
27
10
2020
entrez:
1
6
2020
Statut:
ppublish
Résumé
d-Amino acids are physiologically important components of peptidoglycan in the bacterial cell wall, maintaining cell structure and aiding adaptation to environmental changes through peptidoglycan remodelling. Therefore, the biosynthesis of d-amino acids is essential for bacteria to adapt to different environmental conditions. The peptidoglycan of the extremely thermophilic bacterium Thermus thermophilus contains d-alanine (d-Ala) and d-glutamate (d-Glu), but its d-amino acid metabolism remains poorly understood. Here, we investigated the enzyme activity and function of the product of the TTHA1643 gene, which is annotated to be a Glu racemase in the T. thermophilus HB8 genome. Among 21 amino acids tested, TTHA1643 showed highly specific activity toward Glu as the substrate. The catalytic efficiency (k
Identifiants
pubmed: 32474108
pii: S1570-9639(20)30108-4
doi: 10.1016/j.bbapap.2020.140461
pii:
doi:
Substances chimiques
Amino Acids
0
Recombinant Proteins
0
Glutamic Acid
3KX376GY7L
Amino Acid Isomerases
EC 5.1.1.-
glutamate racemase
EC 5.1.1.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
140461Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no conflict of interest associated with the manuscript.