Literature summary extracted from

Molteni, V.; He, X.; Nabakka, J.; Yang, K.; Kreusch, A.; Gordon, P.; Bursulaya, B.; Warner, I.; Shin, T.; Biorac, T.; Ryder, N.S.; Goldberg, R.; Doughty, J.; He, Y.
Identification of novel potent bicyclic peptide deformylase inhibitors (2004), Bioorg. Med. Chem. Lett., 14, 1477-1481.

Application

EC Number	Application	Comment	Organism
3.5.1.88	medicine	peptide deformylase has been considered an attractive target for antibacterial chemotherapy	Staphylococcus aureus

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.5.1.88	Ni-peptide deformylase from Pseudomonas aeruguinosa was co-crystallized with inhibitor	Staphylococcus aureus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.5.1.88	actinonin	-	Staphylococcus aureus
3.5.1.88	analogues of actinonin	35 different compounds were synthesized and compared to the inhibitory activity of actinonin	Staphylococcus aureus

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
3.5.1.88	Ni	-	Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3.5.1.88	formyl-L-methionyl peptide + H2O	Staphylococcus aureus	-	formate + methionyl peptide	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.88	Staphylococcus aureus	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.5.1.88	formyl-L-methionyl peptide + H2O	-	Staphylococcus aureus	formate + methionyl peptide	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.5.1.88	PDF	-	Staphylococcus aureus
3.5.1.88	peptide deformylase	-	Staphylococcus aureus

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Release 2023.1 (January 2023)