Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-252 binds ATP and competes with ATP-binding at Arg-391, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-252, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (By similarity).
Subject | Predicate | Object | Context |
---|---|---|---|
http://purl.uniprot.org/SHA... | rdf:type | uniprot:Enzyme_Regulation_A... | lld:uniprot |
http://purl.uniprot.org/SHA... | rdfs:comment | Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-252 binds ATP and competes with ATP-binding at Arg-391, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-252, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (By similarity). | lld:uniprot |
uniprot-protein:B3MK83 | uniprot:annotation | http://purl.uniprot.org/SHA... | lld:uniprot |