Characteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum.
Phosphorylation
Glutamic Acid
/ metabolism
Glutamine
/ metabolism
Corynebacterium glutamicum
/ genetics
Ketoglutaric Acids
/ metabolism
Aspartic Acid
/ metabolism
Periplasmic Binding Proteins
/ metabolism
Protein Kinases
/ metabolism
Mycobacterium tuberculosis
/ genetics
Signal Transduction
Bacterial Proteins
/ genetics
Ketoglutarate Dehydrogenase Complex
/ genetics
2-oxoglutarate dehydrogenase
Actinobacteria
Corynebacterium glutamicum
bacterial signaling
forkhead-associated domain
four-helix bundle
periplasmic binding protein
protein phosphorylation
serine/threonine kinases
signal transduction
Journal
Microbiology spectrum
ISSN: 2165-0497
Titre abrégé: Microbiol Spectr
Pays: United States
ID NLM: 101634614
Informations de publication
Date de publication:
21 12 2022
21 12 2022
Historique:
pubmed:
30
11
2022
medline:
28
12
2022
entrez:
29
11
2022
Statut:
ppublish
Résumé
In Corynebacterium glutamicum the protein kinase PknG phosphorylates OdhI and thereby abolishes the inhibition of 2-oxoglutarate dehydrogenase activity by unphosphorylated OdhI. Our previous studies suggested that PknG activity is controlled by the periplasmic binding protein GlnH and the transmembrane protein GlnX, because Δ
Identifiants
pubmed: 36445153
doi: 10.1128/spectrum.02677-22
pmc: PMC9769921
doi:
Substances chimiques
Glutamic Acid
3KX376GY7L
Glutamine
0RH81L854J
Ketoglutaric Acids
0
Aspartic Acid
30KYC7MIAI
Periplasmic Binding Proteins
0
Protein Kinases
EC 2.7.-
Bacterial Proteins
0
Ketoglutarate Dehydrogenase Complex
EC 1.2.4.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0267722Références
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