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Literature summary for 3.5.1.88 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

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

Cloned(Commentary)

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

Crystallization (Commentary)

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

General Stability

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

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can replace Fe2+ without loss of activity, enhances stability Escherichia coli
Co2+ can replace Fe2+ without loss of activity, enhances stability Geobacillus stearothermophilus
Co2+ can replace Fe2+ without loss of activity, enhances stability Pseudomonas aeruginosa
Co2+ can replace Fe2+ without loss of activity, enhances stability Staphylococcus aureus
Fe2+ required Escherichia coli
Fe2+ required Geobacillus stearothermophilus
Fe2+ required Pseudomonas aeruginosa
Fe2+ required Staphylococcus aureus
Ni2+ can replace Fe2+ without loss of activity, enhances stability Escherichia coli
Ni2+ can replace Fe2+ without loss of activity, enhances stability Geobacillus stearothermophilus
Ni2+ can replace Fe2+ without loss of activity, enhances stability Pseudomonas aeruginosa
Ni2+ can replace Fe2+ without loss of activity, enhances stability Staphylococcus aureus

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 involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides formate + L-methionine-polypeptide
-
?
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
-
?
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
-
?
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
-
?
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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?