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Literature summary for 3.5.1.88 extracted from

  • Sharma, A.; Khuller, G.K.; Sharma, S.
    Peptide deformylase--a promising therapeutic target for tuberculosis and antibacterial drug discovery (2009), Expert Opin. Ther. Targets, 13, 753-765.
    View publication on PubMed

Application

Application Comment Organism
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Staphylococcus aureus
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Bacillus subtilis
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Escherichia coli
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Enterobacter cloacae
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Pseudomonas aeruginosa
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Neisseria gonorrhoeae
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Streptococcus pneumoniae
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Klebsiella pneumoniae
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Bacteroides fragilis
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Moraxella catarrhalis
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Staphylococcus epidermidis
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Mycobacterium tuberculosis variant bovis
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Stenotrophomonas maltophilia
medicine peptide deformylase is a therapeutic target for antibacterial drug discovery Enterococcus sp.
medicine peptide deformylase is a therapeutic target for tuberculosis Homo sapiens
medicine peptide deformylase is a therapeutic target for tuberculosis Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
(2R)-N-[(3S)-2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-4,4-dimethylpent-1-en-3-yl]-2-[[formyl(hydroxy)amino]methyl]hexanamide
-
Homo sapiens
(2R)-N-[(3S)-2-[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]-4,4-dimethylpent-1-en-3-yl]-2-[[formyl(hydroxy)amino]methyl]hexanamide
-
Mycobacterium tuberculosis
actinonin
-
Bacillus subtilis
actinonin
-
Bacteroides fragilis
actinonin
-
Enterobacter cloacae
actinonin
-
Enterococcus sp.
actinonin
-
Escherichia coli
actinonin
-
Homo sapiens
actinonin
-
Klebsiella pneumoniae
actinonin
-
Moraxella catarrhalis
actinonin
-
Mycobacterium tuberculosis
actinonin
-
Mycobacterium tuberculosis variant bovis
actinonin
-
Neisseria gonorrhoeae
actinonin
-
Plasmodium falciparum
actinonin
-
Pseudomonas aeruginosa
actinonin
-
Staphylococcus aureus
actinonin
-
Staphylococcus epidermidis
actinonin
-
Stenotrophomonas maltophilia
actinonin
-
Streptococcus pneumoniae
BB-3497
-
Bacillus subtilis
BB-3497
-
Bacteroides fragilis
BB-3497
-
Enterobacter cloacae
BB-3497
-
Enterococcus sp.
BB-3497
-
Escherichia coli
BB-3497
-
Homo sapiens
BB-3497
-
Klebsiella pneumoniae
BB-3497
-
Moraxella catarrhalis
BB-3497
-
Mycobacterium tuberculosis
BB-3497
-
Mycobacterium tuberculosis variant bovis
BB-3497
-
Neisseria gonorrhoeae
BB-3497
-
Plasmodium falciparum
BB-3497
-
Pseudomonas aeruginosa
BB-3497
-
Staphylococcus aureus
BB-3497
-
Staphylococcus epidermidis
BB-3497
-
Stenotrophomonas maltophilia
BB-3497
-
Streptococcus pneumoniae
BB-81384
-
Bacillus subtilis
BB-81384
-
Bacteroides fragilis
BB-81384
-
Enterobacter cloacae
BB-81384
-
Enterococcus sp.
BB-81384
-
Escherichia coli
BB-81384
-
Homo sapiens
BB-81384
-
Klebsiella pneumoniae
BB-81384
-
Moraxella catarrhalis
BB-81384
-
Mycobacterium tuberculosis
BB-81384
-
Mycobacterium tuberculosis variant bovis
BB-81384
-
Neisseria gonorrhoeae
BB-81384
-
Plasmodium falciparum
BB-81384
-
Pseudomonas aeruginosa
BB-81384
-
Staphylococcus aureus
BB-81384
-
Staphylococcus epidermidis
BB-81384
-
Stenotrophomonas maltophilia
BB-81384
-
Streptococcus pneumoniae
BB-83698
-
Bacillus subtilis
BB-83698
-
Bacteroides fragilis
BB-83698
-
Enterobacter cloacae
BB-83698
-
Enterococcus sp.
BB-83698
-
Escherichia coli
BB-83698
-
Homo sapiens
BB-83698
-
Klebsiella pneumoniae
BB-83698
-
Moraxella catarrhalis
BB-83698
-
Mycobacterium tuberculosis
BB-83698
-
Mycobacterium tuberculosis variant bovis
BB-83698
-
Neisseria gonorrhoeae
BB-83698
-
Plasmodium falciparum
BB-83698
-
Pseudomonas aeruginosa
BB-83698
-
Staphylococcus aureus
BB-83698
-
Staphylococcus epidermidis
BB-83698
-
Stenotrophomonas maltophilia
BB-83698
-
Streptococcus pneumoniae
tert-butyl 1-[(2R)-2-[2-(hydroxyamino)-2-oxoethyl]hexanoyl]-L-prolinate
-
Homo sapiens
tert-butyl 1-[(2R)-2-[2-(hydroxyamino)-2-oxoethyl]hexanoyl]-L-prolinate
-
Mycobacterium tuberculosis
VIC-104959 LBM415 Bacillus subtilis
VIC-104959 LBM415 Bacteroides fragilis
VIC-104959 LBM415 Enterobacter cloacae
VIC-104959 LBM415 Enterococcus sp.
VIC-104959 LBM415 Escherichia coli
VIC-104959 LBM415 Homo sapiens
VIC-104959 LBM415 Klebsiella pneumoniae
VIC-104959 LBM415 Moraxella catarrhalis
VIC-104959 LBM415 Mycobacterium tuberculosis
VIC-104959 LBM415 Mycobacterium tuberculosis variant bovis
VIC-104959 LBM415 Neisseria gonorrhoeae
VIC-104959 LBM415 Plasmodium falciparum
VIC-104959 LBM415 Pseudomonas aeruginosa
VIC-104959 LBM415 Staphylococcus aureus
VIC-104959 LBM415 Staphylococcus epidermidis
VIC-104959 LBM415 Stenotrophomonas maltophilia
VIC-104959 LBM415 Streptococcus pneumoniae
VRC-3375
-
Bacillus subtilis
VRC-3375
-
Bacteroides fragilis
VRC-3375
-
Enterobacter cloacae
VRC-3375
-
Enterococcus sp.
VRC-3375
-
Escherichia coli
VRC-3375
-
Homo sapiens
VRC-3375
-
Klebsiella pneumoniae
VRC-3375
-
Moraxella catarrhalis
VRC-3375
-
Mycobacterium tuberculosis
VRC-3375
-
Mycobacterium tuberculosis variant bovis
VRC-3375
-
Neisseria gonorrhoeae
VRC-3375
-
Plasmodium falciparum
VRC-3375
-
Pseudomonas aeruginosa
VRC-3375
-
Staphylococcus aureus
VRC-3375
-
Staphylococcus epidermidis
VRC-3375
-
Stenotrophomonas maltophilia
VRC-3375
-
Streptococcus pneumoniae
VRC-4307
-
Bacillus subtilis
VRC-4307
-
Bacteroides fragilis
VRC-4307
-
Enterobacter cloacae
VRC-4307
-
Enterococcus sp.
VRC-4307
-
Escherichia coli
VRC-4307
-
Homo sapiens
VRC-4307
-
Klebsiella pneumoniae
VRC-4307
-
Moraxella catarrhalis
VRC-4307
-
Mycobacterium tuberculosis
VRC-4307
-
Mycobacterium tuberculosis variant bovis
VRC-4307
-
Neisseria gonorrhoeae
VRC-4307
-
Plasmodium falciparum
VRC-4307
-
Pseudomonas aeruginosa
VRC-4307
-
Staphylococcus aureus
VRC-4307
-
Staphylococcus epidermidis
VRC-4307
-
Stenotrophomonas maltophilia
VRC-4307
-
Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-formyl-L-methionine-polypeptide + H2O Staphylococcus aureus
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Bacillus subtilis
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Escherichia coli
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Homo sapiens
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Enterobacter cloacae
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Pseudomonas aeruginosa
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Neisseria gonorrhoeae
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Streptococcus pneumoniae
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Klebsiella pneumoniae
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Mycobacterium tuberculosis
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Bacteroides fragilis
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Moraxella catarrhalis
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Staphylococcus epidermidis
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Plasmodium falciparum
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Mycobacterium tuberculosis variant bovis
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Stenotrophomonas maltophilia
-
formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O Enterococcus sp.
-
formate + L-methionine-polypeptide
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacteroides fragilis
-
-
-
Enterobacter cloacae
-
-
-
Enterococcus sp.
-
-
-
Escherichia coli
-
-
-
Homo sapiens
-
-
-
Klebsiella pneumoniae
-
-
-
Moraxella catarrhalis
-
-
-
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis variant bovis
-
-
-
Neisseria gonorrhoeae
-
-
-
Plasmodium falciparum
-
-
-
Pseudomonas aeruginosa
-
-
-
Staphylococcus aureus
-
-
-
Staphylococcus epidermidis
-
-
-
Stenotrophomonas maltophilia
-
-
-
Streptococcus pneumoniae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-formyl-L-methionine-polypeptide + H2O
-
Staphylococcus aureus formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Bacillus subtilis formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Escherichia coli formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Homo sapiens formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Enterobacter cloacae formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Pseudomonas aeruginosa formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Neisseria gonorrhoeae formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Streptococcus pneumoniae formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Klebsiella pneumoniae formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Mycobacterium tuberculosis formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Bacteroides fragilis formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Moraxella catarrhalis formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Staphylococcus epidermidis formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Plasmodium falciparum formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Mycobacterium tuberculosis variant bovis formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Stenotrophomonas maltophilia formate + L-methionine-polypeptide
-
?
N-formyl-L-methionine-polypeptide + H2O
-
Enterococcus sp. formate + L-methionine-polypeptide
-
?

Synonyms

Synonyms Comment Organism
PDF
-
Staphylococcus aureus
PDF
-
Bacillus subtilis
PDF
-
Escherichia coli
PDF
-
Homo sapiens
PDF
-
Enterobacter cloacae
PDF
-
Pseudomonas aeruginosa
PDF
-
Neisseria gonorrhoeae
PDF
-
Streptococcus pneumoniae
PDF
-
Klebsiella pneumoniae
PDF
-
Mycobacterium tuberculosis
PDF
-
Bacteroides fragilis
PDF
-
Moraxella catarrhalis
PDF
-
Staphylococcus epidermidis
PDF
-
Plasmodium falciparum
PDF
-
Mycobacterium tuberculosis variant bovis
PDF
-
Stenotrophomonas maltophilia
PDF
-
Enterococcus sp.

General Information

General Information Comment Organism
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Staphylococcus aureus
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Bacillus subtilis
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Escherichia coli
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Homo sapiens
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Enterobacter cloacae
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Pseudomonas aeruginosa
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Neisseria gonorrhoeae
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Streptococcus pneumoniae
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Klebsiella pneumoniae
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Mycobacterium tuberculosis
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Bacteroides fragilis
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Moraxella catarrhalis
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Staphylococcus epidermidis
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Plasmodium falciparum
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Mycobacterium tuberculosis variant bovis
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Stenotrophomonas maltophilia
physiological function PDF plays a critical role in mediating the maturation process of the nascent polypeptides partly due to the necessity of removing the N-formyl group to render nascent polypeptides available for cleavage of the N-terminal methionine residue by methionine amino peptidase Enterococcus sp.