Literature summary extracted from

Becker, A.; Schlichting, I.; Kabsch, W.; Groche, D.; Schultz, S.; Wagner, A.F.V.
Iron center, substrate recognition and mechanism of peptide deformylase (1998), Nature Struct. Biol., 5, 1053-1058.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.5.1.88	Fe2+-, Ni2+- and Zn2+-bound enzyme, Met-Ala-Ser-tripeptide bound to the substrate binding-site	Escherichia coli

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
3.5.1.88	Fe2+	-	Escherichia coli
3.5.1.88	Ni2+	-	Escherichia coli
3.5.1.88	Zn2+	Zn2+-bound enzyme inactive in crystallization analysis	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.88	Escherichia coli	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.5.1.88	additional information	proposed reaction cycle of peptide deformylase	Escherichia coli	?	-	?
3.5.1.88	N-formyl-Met + H2O	minimal substrate	Escherichia coli	formate + Met	-	?
3.5.1.88	N-formyl-Met-Ala + H2O	-	Escherichia coli	formate + Met-Ala	-	?

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Release 2023.1 (January 2023)