Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.88 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.
    View publication on PubMed

Crystallization (Commentary)

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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