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Literature summary for 3.5.1.88 extracted from

  • Han, J.H.; Choi, Y.S.; Kim, W.J.; Jeon, Y.H.; Lee, S.K.; Lee, B.J.; Ryu, K.S.
    Codon optimization enhances protein expression of human peptide deformylase in E. coli (2010), Protein Expr. Purif., 70, 224-230.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
GST-tagged original PDF protein and thioredoxin-tagged original PDF are expressed in both Escherichia coli BL21 (DE3) and Rosetta (DE3) strains, respectively Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
actinonin efficient inhibitor Homo sapiens
additional information purified thioredoxin-fused PDF containing Fe2+ ion is inactivated during purification Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Co2+ is an optimal metal for increasing the activity of purified thioredoxin-fused PDF Homo sapiens
Fe2+ only Fe2+ and Co2+ ions are capable of supporting the enzyme activity of PDF Homo sapiens
additional information Zn2+ and Ni2+ are not capable of supporting the enzyme activity of PDF Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione Sepharose column chromatography and Ni Sepharose column chromatography Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PDF
-
Homo sapiens