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

BRENDA support

Literature summary for 3.5.1.88 extracted from

  • Amero, C.D.; Byerly, D.W.; McElroy, C.A.; Simmons, A.; Foster, M.P.
    Ligand-induced changes in the structure and dynamics of Escherichia coli peptide deformylase (2009), Biochemistry, 48, 7595-7607.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.88

Inhibitors

Inhibitors Comment Organism Structure
actinonin i.e. 3-[(1-[[2-(hydroxymethyl)-1-pyrrolidinyl]carbonyl]-2-methylpropyl)carbamoyl]octanohydroxamic acid, a naturally occurring potent PDF inhibitor Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the native metal in Escherichia coli PDF is iron Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-formyl-L-methionine-polypeptide + H2O Escherichia coli
-
 formate + L-methionine-polypeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6K3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-L-methionine-polypeptide + H2O
-
 Escherichia coli formate + L-methionine-polypeptide
-
 ?

Synonyms

Synonyms Comment Organism
PDF
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function PDF is an essential and highly conserved enzyme that functions in protein maturation by removing the N-formyl group from the methionine of nascently synthesized polypeptides Escherichia coli