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Literature summary extracted from

  • Guilloteau, J.P.; Mathieu, M.; Giglione, C.; Blanc, V.; Dupuy, A.; Chevrier, M.; Gil, P.; Famechon, A.; Meinnel, T.; Mikol, V.
    The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents (2002), J. Mol. Biol., 320, 951-962.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.88 drug development potential target or the development of new antibacterial agents Escherichia coli
3.5.1.88 drug development potential target or the development of new antibacterial agents Geobacillus stearothermophilus
3.5.1.88 drug development potential target or the development of new antibacterial agents Pseudomonas aeruginosa
3.5.1.88 drug development potential target or the development of new antibacterial agents Staphylococcus aureus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.88 expressed in an Escherichia coli deficiency strain Pseudomonas aeruginosa
3.5.1.88 expressed in an Escherichia coli deficiency strain Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.88 vapor diffusion method Escherichia coli
3.5.1.88 vapor diffusion method Geobacillus stearothermophilus
3.5.1.88 vapor diffusion method Pseudomonas aeruginosa
3.5.1.88 vapor diffusion method Staphylococcus aureus

General Stability

EC Number General Stability Organism
3.5.1.88 Ni2+ and Co2+ increase stability compared to the Fe2+ enzyme Geobacillus stearothermophilus
3.5.1.88 Ni2+ and Co2+ increase stability compared to the Fe2+ enzyme Pseudomonas aeruginosa
3.5.1.88 Ni2+ and Co2+ increase stability compared to the Fe2+ enzyme Staphylococcus aureus
3.5.1.88 Ni2+ and Co2+ increases stability compared to the Fe2+ enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.88 actinonin
-
 Escherichia coli
3.5.1.88 actinonin
-
 Geobacillus stearothermophilus
3.5.1.88 actinonin
-
 Pseudomonas aeruginosa
3.5.1.88 actinonin
-
 Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.88 Co2+ can replace Fe2+ without loss of activity, enhances stability Escherichia coli
3.5.1.88 Co2+ can replace Fe2+ without loss of activity, enhances stability Geobacillus stearothermophilus
3.5.1.88 Co2+ can replace Fe2+ without loss of activity, enhances stability Pseudomonas aeruginosa
3.5.1.88 Co2+ can replace Fe2+ without loss of activity, enhances stability Staphylococcus aureus
3.5.1.88 Fe2+ required Escherichia coli
3.5.1.88 Fe2+ required Geobacillus stearothermophilus
3.5.1.88 Fe2+ required Pseudomonas aeruginosa
3.5.1.88 Fe2+ required Staphylococcus aureus
3.5.1.88 Ni2+ can replace Fe2+ without loss of activity, enhances stability Escherichia coli
3.5.1.88 Ni2+ can replace Fe2+ without loss of activity, enhances stability Geobacillus stearothermophilus
3.5.1.88 Ni2+ can replace Fe2+ without loss of activity, enhances stability Pseudomonas aeruginosa
3.5.1.88 Ni2+ can replace Fe2+ without loss of activity, enhances stability 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 N-formyl-L-methionine-polypeptide + H2O Escherichia coli involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O Geobacillus stearothermophilus involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O Pseudomonas aeruginosa involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O Staphylococcus aureus involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O Staphylococcus aureus RN4220 involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides formate + L-methionine-polypeptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.88 Escherichia coli P0A6K3
-
-
3.5.1.88 Geobacillus stearothermophilus O31410
-
-
3.5.1.88 Pseudomonas aeruginosa Q9I7A8 strain ATCC27853
-
3.5.1.88 Staphylococcus aureus P68826
-
-
3.5.1.88 Staphylococcus aureus RN4220 P68826
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.88
-
 Escherichia coli
3.5.1.88
-
 Geobacillus stearothermophilus
3.5.1.88 recombinant enzyme Pseudomonas aeruginosa
3.5.1.88 recombinant enzyme Staphylococcus aureus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides Escherichia coli formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides Geobacillus stearothermophilus formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides Pseudomonas aeruginosa formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides Staphylococcus aureus formate + L-methionine-polypeptide
-
 ?
3.5.1.88 N-formyl-L-methionine-polypeptide + H2O involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides Staphylococcus aureus RN4220 formate + L-methionine-polypeptide
-
 ?