Literature summary extracted from

Spyrakis, F.; Felici, P.; Bayden, A.S.; Salsi, E.; Miggiano, R.; Kellogg, G.E.; Cozzini, P.; Cook, P.F.; Mozzarelli, A.; Campanini, B.
Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase (2013), Biochim. Biophys. Acta, 1834, 169-181.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.5.1.47	additional information	activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction	Haemophilus influenzae
2.5.1.47	additional information	activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction	Salmonella enterica

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.5.1.47	Haemophilus influenzae	P45040	-	-
2.5.1.47	Salmonella enterica	P0A1E3	subsp. enterica serovar Typhimurium	-

Synonyms

EC Number	Synonyms	Comment	Organism
2.5.1.47	OASS	-	Haemophilus influenzae
2.5.1.47	OASS	-	Salmonella enterica

General Information

EC Number	General Information	Comment	Organism
2.5.1.47	physiological function	activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction	Haemophilus influenzae
2.5.1.47	physiological function	activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction	Salmonella enterica

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Release 2023.1 (January 2023)