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Literature summary for 2.3.1.87 extracted from

  • Aboalroub, A.A.; Bachman, A.B.; Zhang, Z.; Keramisanou, D.; Merkler, D.J.; Gelis, I.
    Acetyl group coordinated progression through the catalytic cycle of an arylalkylamine N-acetyltransferase (2017), PLoS ONE, 12, e0177270 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bombyx mori

Organism

Organism UniProt Comment Textmining
Bombyx mori
-
-
-

Synonyms

Synonyms Comment Organism
AANAT3
-
Bombyx mori

General Information

General Information Comment Organism
physiological function CoA and acetyl-CoA alter the conformation of the substrate binding site of arylalkylamine N-acetyltransferase to facilitate interaction with acceptor substrates. It is the presence of the acetyl group within the catalytic funnel that triggers high affinity binding. Acetyl group occupancy is relayed through a conserved salt bridge between the P-loop and the acceptor binding site, and is manifested as differential dynamics in the CoA and acetyl-CoA-bound states Bombyx mori