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Literature summary for 2.7.2.8 extracted from

  • Marcos, E.; Crehuet, R.; Bahar, I.
    Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members (2011), PLoS Comput. Biol., 7(9), e1002201.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate using an elastic network model representation a normal mode analysis shows that the conformational mechanisms for substrate binding by NAGK strongly correlate with the intrinsic dynamics of the enzyme in the unbound form. The conformational change observed between the open and closed forms of EcNAGK are essentially accomplished by movements along a small subset of modes Escherichia coli

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
EcNAGK
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Escherichia coli