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formyl-L-methionyl peptide + H2O
formate + methionyl peptide
-
-
-
?
formyl-MAHA + H2O
formate + MAHA
peptide substrate derived from mitochondrial cytochrome c oxidase subunit II
-
-
?
formyl-MEHQ + H2O
formate + MEHQ
-
-
-
?
formyl-Met-Ala-His-Ala + H2O
formate + methionyl-Ala-His-Ala
fMAHA
-
-
?
formyl-Met-Ala-Ser + H2O
formate + Met-Ala-Ser
formyl-Met-Thr-Met-His + H2O
formate + methionyl-Thr-Met-His
fMTMH
-
-
?
formyl-MFAD + H2O
formate + MFAD
peptide substrate derived from mitochondrial cytochrome c oxidase subunit I
-
-
?
formyl-MFHQ + H2O
formate + MMFQ
-
-
-
?
formyl-MGHQ + H2O
formate + MGHQ
-
-
-
?
formyl-MLHQ + H2O
formate + MLHQ
-
-
-
?
formyl-MLKL + H2O
formate + MLKL
peptide substrate derived from mitochondrial NADH dehydrogenase subunit 4
-
-
?
formyl-MMYA + H2O
formate + MMYA
peptide substrate derived from mitochondrial NADH dehydrogenase subunit 6
-
-
?
formyl-MNFA + H2O
formate + MNFA
peptide substrate derived from mitochondrial NADH dehydrogenase subunit 3
-
-
?
formyl-MNPL + H2O
formate + MNPL
peptide substrate derived from mitochondrial NADH dehydrogenase subunit 2
-
-
?
formyl-MPQL + H2O
formate + MPQL
peptide substrate derived from mitochondrial ATP synthase F0 subunit 8
-
-
?
formyl-MRHQ + H2O
formate + MRHQ
-
-
-
?
formyl-MTHQ + H2O
formate + MTHQ
formyl-MTMH + H2O
formate + MTMH
peptide substrate derived from mitochondrial NADH dehydrogenase subunit 5
-
-
?
formyl-MTPM + H2O
formate + MTPM
peptide substrate derived from mitochondrial cytochrome b
-
-
?
formyl-MVHQ + H2O
formate + MVHQ
-
-
-
?
formyl-L-Met-Leu-p-nitroanilide + H2O
formate + Met-Leu-p-nitroanilide
-
-
-
-
?
formyl-Met-Ala-His-Ala-Ala-Gln + H2O
formate + Met-Ala-His-Ala-Ala-Gln
-
-
-
-
?
formyl-Met-Ala-Ser + H2O
formate + Met-Ala-Ser
-
-
-
-
?
formyl-Met-Leu-p-nitroanilide + H2O
formate + Met-Leu-p-nitroanilide
-
-
-
-
?
formyl-Met-Thr-Gln-Ser-His + H2O
formate + Met-Thr-Gln-Ser-His
-
-
-
-
?
formyl-Met-Thr-Met-His-Thr-Thr + H2O
formate + Met-Thr-Met-His-Thr-Thr
-
-
-
-
?
N-formyl-L-methionine polypeptide + H2O
formate + methionine-polypeptide
-
-
-
-
?
N-formyl-L-methionine-polypeptide + H2O
formate + L-methionine-polypeptide
-
-
-
-
?
additional information
?
-
formyl-Met-Ala-Ser + H2O
formate + Met-Ala-Ser
-
-
-
?
formyl-Met-Ala-Ser + H2O
formate + Met-Ala-Ser
fMAS
-
-
?
formyl-MTHQ + H2O
formate + MTHQ
-
-
-
?
formyl-MTHQ + H2O
formate + MTHQ
peptide substrate derived from mitochondrial cytochrome c oxidase subunit III
-
-
?
additional information
?
-
HsPDF can process, in vitro, N-Met-formylated peptides
-
-
?
additional information
?
-
-
HsPDF can process, in vitro, N-Met-formylated peptides
-
-
?
additional information
?
-
-
no activity with formyl-Met-Thr-Pro-Met-Arg-Lys
-
-
?
additional information
?
-
-
no detectable activity with formyl-Met-Leu-Phe and formyl-Met-Leu-Pro
-
-
?
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(2R)-N4-hydroxy-N1-[(2S)-3-methyl-1-oxo-1-(piperidin-1-yl)butan-2-yl]-2-pentylbutanediamide
-
1-(5-bromo-2-methyl-1H-indol-3-yl)-N-hydroxymethanamine
-
1-[5-bromo-2-methyl-1-(phenylsulfonyl)-1H-indol-3-yl]-N-hydroxymethanamine
-
2-(2-ethoxy-4-(((4-(3-oxomorpholino)phenyl)amino)methyl)phenoxy)-N-hydroxyacetamide
the compound exhibits potent anticancer activities against HeLa, A549 and MCF-7 cell lines with IC50s of 0.0364, 0.120, and 0.0480 mM, respectively
2-(2-ethoxy-4-((morpholinoamino)methyl)phenoxy)-N-hydroxyacetamide
the compound exhibits potent anticancer activities against HeLa, A549 and MCF-7 cell lines with IC50s of 0.0096, 0.0679, and 0.0229 mM, respectively
2-(2-ethoxy-4-((pyridin-3-ylamino)methyl)phenoxy)-N-hydroxyacetamide
the compound exhibits potent anticancer activities against HeLa, A549 and MCF-7 cell lines with IC50s of 0.0966, 0.0454, and 0.0136 mM, respectively
2-(4-fluoro-1H-indol-3-yl)-N-hydroxyacetamide
-
2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide
2-(5-bromo-2-methyl-1H-indol-3-yl)-N-hydroxyacetamide
-
2-(5-chloro-1H-indol-3-yl)-N-hydroxyacetamide
-
2-(5-fluoro-1H-indol-3-yl)-N-hydroxyacetamide
-
2-(6-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
2-[2-chloro-4-([[2-(1H-indol-3-yl)ethyl]amino]methyl)-6-methoxyphenoxy]acetamide
i.e. M7594_0037, the compound exhibits potent anticancer activities against HeLa, A549 and MCF-7 cell lines with IC50s of 0.0353, 0.0296, and 0.0246 mM, respectively
6,7-dibromo-3-(3,4-dimethoxy-5-methylbenzoyl)-1-benzofuran-4(5H)-one
-
6,7-dichloro-3-(3,4-dimethoxybenzoyl)-1-benzofuran-4,5-dione
-
benzyl 5-bromo-3-[2-(hydroxyamino)-2-oxoethyl]-1H-indole-1-carboxylate
-
ethyl 1-(N-[(2R)-2-[2-(hydroxyamino)-2-oxoethyl]heptanoyl]-L-valyl)piperidine-3-carboxylate
-
ethyl 2-(2-ethoxy-4-(((4-(3-oxomorpholino)phenyl)amino)methyl)phenoxy)acetate
-
ethyl 2-(2-ethoxy-4-((morpholinoamino)methyl)phenoxy)acetate
-
ethyl 2-(2-ethoxy-4-formylphenoxy)acetate
-
N-hydroxy-2-(1H-indol-3-yl)acetamide
-
N-hydroxy-2-(5-methoxy-1H-indol-3-yl)acetamide
-
N-[(3,5-difluorophenyl)carbamoyl]-3-methyl-L-valyl-N2-cyclopentyl-N-hydroxyglycinamide
cytotoxic IC50 values for compound PMT497 are 0.0209 mM against MDA-MB-231 and 0.0212 mM against MDA-MB-468 cell lines
N-[[5-bromo-2-methyl-1-(phenylsulfonyl)-1H-indol-3-yl]methyl]-N-hydroxyformamide
-
siRNA HsPDF 581-601
transfection of HeLa cells
-
siRNA HsPDF 659-679
transfection of HeLa cells
-
SKI-AC-1
IC50: 0.000072 mM, actionin analog
SKI-AC-10
IC50: 0.000078 mM, actionin analog
SKI-AC-11101
IC50: 0.000076 mM, actionin analog
-
SKI-AC-111101
IC50: 0.0000600 mM, actionin analog
SKI-AC-111110
IC50: 0.000427 mM, actionin analog
-
SKI-AC-111111
IC50: 0.000069 mM, actionin analog
SKI-AC-111112
IC50: 0.000234 mM, actionin analog
-
SKI-AC-111113
IC50: 0.000177 mM, actionin analog
-
SKI-AC-111114
IC50: 0.000300 mM, actionin analog
-
SKI-AC-11112
IC50: 0.000365 mM, actionin analog
-
SKI-AC-11113
IC50: 0.000500 mM, actionin analog
-
SKI-AC-11114
IC50: 0.000276 mM, actionin analog
-
SKI-AC-11115
IC50: 0.000473 mM, actionin analog
-
SKI-AC-11116
IC50: 0.000335 mM, actionin analog
-
SKI-AC-11117
IC50: 0.000086 mM, actionin analog
SKI-AC-11118
IC50: 0.000115 mM, actionin analog
SKI-AC-11119
IC50: 0.000134 mM, actionin analog
-
SKI-AC-11128
IC50: 0.000522 mM, actionin analog
-
SKI-AC-11138
IC50: 0.000500 mM, actionin analog
-
SKI-AC-11148
IC50: 0.0000600 mM, actionin analog
-
SKI-AC-11158
IC50: 0.000500 mM, actionin analog
-
SKI-AC-11168
IC50: 0.000192 mM, actionin analog
-
SKI-AC-11178
IC50: 0.000200 mM, actionin analog
-
SKI-AC-11188
IC50: 0.000120 mM, actionin analog
SKI-AC-11198
IC50: 0.000090 mM, actionin analog
SKI-AC-3
IC50: 0.000500 mM, actionin analog
-
SKI-AC-5
IC50: 0.000400 mM, actionin analog
-
SKI-AC-51121
IC50: 0.000400 mM, actionin analog
-
SKI-AC-6
IC50: 0.000097 mM, actionin analog
SKI-AC-8
IC50: 0.000093 mM, actionin analog
SKI-AC-9
IC50: 0.000151 mM, actionin analog
-
SKI-AC-I-18
IC50: 0.000404 mM, actionin analog
-
SKI-AC-I-19
IC50: 0.000239 mM, actionin analog
-
(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
-
-
(R)-2-[(formyl-hydroxy-amino)-methyl]-hexanoic acid ((S)-5-amino-1-phenylcarbamoyl-pentyl)-amide
-
-
(R)-2-[(formyl-hydroxy-amino)-methyl]-hexanoic acid [(S)-5-amino-1-((R)-2-isopropoxymethyl-pyrrolidine-1-carbonyl)-pentyl]-amide
-
-
(R)-2-[(formyl-hydroxy-amino)-methyl]-hexanoic acid [(S)-5-amino-1-((S)-2-isopropoxymethyl-pyrrolidine-1-carbonyl)-pentyl]-amide
-
-
2',2'-bisepigallocatechin monogallate
-
-
2-(4-fluoro-1H-indol-3-yl)-N-hydroxyacetamide
-
-
2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
-
2-(5-bromo-2-methyl-1H-indolyl)-N-hydroxyacetamide
-
-
2-(5-chloro-1H-indol-3-yl)-N-hydroxyacetamide
-
-
2-(6-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
-
epigallocatechin 3,5-digallate
-
-
epitheaflavin monogallate
-
-
N-(1-benzenesulfonyl-5-bromo-2-methyl-1H-indol-3-ylmethyl)-N-hydroxyformamide
-
-
tert-butyl 1-[(2R)-2-[2-(hydroxyamino)-2-oxoethyl]hexanoyl]-L-prolinate
-
-
theaflavin monogallate
-
-
2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
-
actinonin
-
actinonin
IC50: 0.000043 mM
actinonin
binding structure to the enzyme, overview
actinonin
enzyme inhibitor, inhibits the growth of both cancer and non-cancer cell lines
actinonin
-
-
actinonin
-
efficient inhibitor
actinonin
-
competitive, IC50: 43 nM
additional information
different classes of PDF inhibitors, structures, and molecular modeling studies, overview
-
additional information
-
different classes of PDF inhibitors, structures, and molecular modeling studies, overview
-
additional information
structure-based drug design of small molecule peptide deformylase inhibitors to treat cancer, molecular docking studies revealing that M7594_0037 and its three derivatives interact with HsPDF by several conserved hydrogen bonds. Compound synthesis using the crystal structure of the HsPDF complex with actinonin (PDB ID 3G5K) as template
-
additional information
-
structure-based drug design of small molecule peptide deformylase inhibitors to treat cancer, molecular docking studies revealing that M7594_0037 and its three derivatives interact with HsPDF by several conserved hydrogen bonds. Compound synthesis using the crystal structure of the HsPDF complex with actinonin (PDB ID 3G5K) as template
-
additional information
-
development of a high-throughput assay to screen for inhibitors
-
additional information
-
purified thioredoxin-fused PDF containing Fe2+ ion is inactivated during purification
-
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Anemia, Hypochromic
Inhibition of peptide deformylase in Nicotiana tabacum leads to decreased D1 protein accumulation, ultimately resulting in a reduction of photosystem II complexes
Anemia, Hypochromic
Inhibition of peptide deformylase in Nicotiana tabacum leads to decreased D1 protein accumulation, ultimately resulting in a reduction of photosystem II complexes.
Bacterial Infections
Chronicles in drug discovery.
Burkitt Lymphoma
Inhibition of human mitochondrial peptide deformylase causes apoptosis in c-myc-overexpressing hematopoietic cancers.
Infections
A Repurposing Approach for Uncovering the Anti-Tubercular Activity of FDA-Approved Drugs with Potential Multi-Targeting Profiles.
Infections
Antimicrobial activity of a novel peptide deformylase inhibitor, LBM415, tested against respiratory tract and cutaneous infection pathogens: a global surveillance report (2003-2004).
Infections
Comparative Analysis of the Antibacterial Activity of a Novel Peptide Deformylase Inhibitor, GSK1322322.
Infections
Comparative antimicrobial characterization of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance.
Infections
Determination of disk diffusion and MIC quality control ranges for GSK1322322, a novel peptide deformylase inhibitor.
Infections
Discovery of piperazic acid peptide deformylase inhibitors with in vivo activity for respiratory tract and skin infections.
Infections
Disk diffusion quality control guidelines for NVP-PDF 713: a novel peptide deformylase inhibitor.
Infections
In vivo characterization of the peptide deformylase inhibitor LBM415 in murine infection models.
Infections
Inhibition of chlamydial infection in the genital tract of female mice by topical application of a peptide deformylase inhibitor.
Infections
Oral anti-pneumococcal activity and pharmacokinetic profiling of a novel peptide deformylase inhibitor.
Infections
Pharmacokinetics and tolerability of IDP-73152 mesylate after a single oral administration under fasted and fed conditions in healthy volunteers.
Infections
Pharmacokinetics/Pharmacodynamics of Peptide Deformylase Inhibitor GSK1322322 against Streptococcus pneumoniae, Haemophilus influenzae, and Staphylococcus aureus in Rodent Models of Infection.
Infections
Potential utility of a peptide deformylase inhibitor (NVP PDF-713) against oxazolidinone-resistant or streptogramin-resistant Gram-positive organism isolates.
Infections
Quantification of IDP-73152, a novel antibiotic, in plasma from mice, rats and humans using an ultra-high performance liquid chromatography/tandem mass spectrometry method for use in pharmacokinetic studies.
Leukemia, Myeloid, Acute
Inhibition of human mitochondrial peptide deformylase causes apoptosis in c-myc-overexpressing hematopoietic cancers.
Lung Neoplasms
Overexpression of peptide deformylase in breast, colon, and lung cancers.
Malaria
An improved crystal form of Plasmodium falciparum peptide deformylase.
Neoplasms
A new human peptide deformylase inhibitable by actinonin.
Neoplasms
Chronicles in drug discovery.
Neoplasms
High-throughput identification of inhibitors of human mitochondrial peptide deformylase.
Neoplasms
Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics.
Neoplasms
Inhibition of human mitochondrial peptide deformylase causes apoptosis in c-myc-overexpressing hematopoietic cancers.
Neoplasms
Overexpression of peptide deformylase in breast, colon, and lung cancers.
Neoplasms
Peptide deformylase inhibitor actinonin reduces celastrol's HSP70 induction while synergizing proliferation inhibition in tumor cells.
Neoplasms
Structure and activity of human mitochondrial peptide deformylase, a novel cancer target.
Neoplasms
Structure-Based Drug Design of Small Molecule Peptide Deformylase Inhibitors to Treat Cancer.
Neoplasms
Synthesis and Anticancer Activity of Novel Actinonin Derivatives as HsPDF Inhibitors.
Pneumonia
Comparative Analysis of the Antibacterial Activity of a Novel Peptide Deformylase Inhibitor, GSK1322322.
Pneumonia
Determination of disk diffusion and MIC quality control ranges for GSK1322322, a novel peptide deformylase inhibitor.
Pneumonia
Efficacy of BB-83698, a novel peptide deformylase inhibitor, in a mouse model of pneumococcal pneumonia.
Pneumonia
Evaluation of LBM415 (NVP PDF-713), a novel peptide deformylase inhibitor, for treatment of experimental Mycoplasma pneumoniae pneumonia.
Pneumonia
Pharmacokinetics/Pharmacodynamics of Peptide Deformylase Inhibitor GSK1322322 against Streptococcus pneumoniae, Haemophilus influenzae, and Staphylococcus aureus in Rodent Models of Infection.
Pneumonia, Bacterial
In vitro and intracellular activities of peptide deformylase inhibitor GSK1322322 against Legionella pneumophila isolates.
Pneumonia, Pneumococcal
Efficacy of BB-83698, a novel peptide deformylase inhibitor, in a mouse model of pneumococcal pneumonia.
Respiratory Tract Diseases
Comparative antimicrobial characterization of LBM415 (NVP PDF-713), a new peptide deformylase inhibitor of clinical importance.
Respiratory Tract Infections
Antimicrobial activity of a novel peptide deformylase inhibitor, LBM415, tested against respiratory tract and cutaneous infection pathogens: a global surveillance report (2003-2004).
Respiratory Tract Infections
Disk diffusion quality control guidelines for NVP-PDF 713: a novel peptide deformylase inhibitor.
Respiratory Tract Infections
Pharmacokinetics and tolerability of IDP-73152 mesylate after a single oral administration under fasted and fed conditions in healthy volunteers.
Soft Tissue Infections
Antimicrobial activity of a novel peptide deformylase inhibitor, LBM415, tested against respiratory tract and cutaneous infection pathogens: a global surveillance report (2003-2004).
Tuberculosis
A Repurposing Approach for Uncovering the Anti-Tubercular Activity of FDA-Approved Drugs with Potential Multi-Targeting Profiles.
Tuberculosis
BB-3497, a peptide deformylase inhibitor, is active against Mycobacterium tuberculosis.
Tuberculosis
Carfilzomib as a potential inhibitor of NADH-dependent enoyl-acyl carrier protein reductases of Klebsiella pneumoniae and Mycobacterium tuberculosis as a drug target enzyme: insights from molecular docking and molecular dynamics.
Tuberculosis
Glycine in the conserved motif III modulates the thermostability and oxidative stress resistance of peptide deformylase in Mycobacterium tuberculosis.
Tuberculosis
Identification of regions involved in enzymatic stability of peptide deformylase of Mycobacterium tuberculosis.
Tuberculosis
In vitro and ex vivo activity of peptide deformylase inhibitors against Mycobacterium tuberculosis H37Rv.
Tuberculosis
Novel peptidomimetic peptide deformylase (PDF) inhibitors of Mycobacterium tuberculosis.
Tuberculosis
Peptide deformylase inhibitors of Mycobacterium tuberculosis: synthesis, structural investigations, and biological results.
Tuberculosis
Peptide deformylase--a promising therapeutic target for tuberculosis and antibacterial drug discovery.
Tuberculosis
The carboxy-terminal end of the peptide deformylase from Mycobacterium tuberculosis is indispensable for its enzymatic activity.
Tuberculosis
Therapeutic potential of peptide deformylase inhibitors against experimental tuberculosis.
Tuberculosis
Three consecutive arginines are important for the mycobacterial peptide deformylase enzyme activity.
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0.000115
(2R)-N4-hydroxy-N1-[(2S)-3-methyl-1-oxo-1-(piperidin-1-yl)butan-2-yl]-2-pentylbutanediamide
pH and temperature not specified in the publication
0.36
2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide
pH and temperature not specified in the publication
0.0052
6,7-dibromo-3-(3,4-dimethoxy-5-methylbenzoyl)-1-benzofuran-4(5H)-one
pH and temperature not specified in the publication
0.0061
6,7-dichloro-3-(3,4-dimethoxybenzoyl)-1-benzofuran-4,5-dione
pH and temperature not specified in the publication
0.000069
ethyl 1-(N-[(2R)-2-[2-(hydroxyamino)-2-oxoethyl]heptanoyl]-L-valyl)piperidine-3-carboxylate
pH and temperature not specified in the publication
0.0027
hematoxylin
pH and temperature not specified in the publication
0.0088
puppurogallin
pH and temperature not specified in the publication
0.0061
theaflavin
pH and temperature not specified in the publication
0.00015
(R)-2-[(formyl-hydroxy-amino)-methyl]-hexanoic acid ((S)-5-amino-1-phenylcarbamoyl-pentyl)-amide
-
-
0.000045
(R)-2-[(formyl-hydroxy-amino)-methyl]-hexanoic acid [(S)-5-amino-1-((R)-2-isopropoxymethyl-pyrrolidine-1-carbonyl)-pentyl]-amide
-
-
0.000036
(R)-2-[(formyl-hydroxy-amino)-methyl]-hexanoic acid [(S)-5-amino-1-((S)-2-isopropoxymethyl-pyrrolidine-1-carbonyl)-pentyl]-amide
-
-
0.7
2-(4-fluoro-1H-indol-3-yl)-N-hydroxyacetamide
-
-
0.36
2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
-
0.45
2-(5-bromo-2-methyl-1H-indolyl)-N-hydroxyacetamide
-
-
0.6
2-(5-chloro-1H-indol-3-yl)-N-hydroxyacetamide
-
-
0.25
2-(6-bromo-1H-indol-3-yl)-N-hydroxyacetamide
-
-
0.2
N-(1-benzenesulfonyl-5-bromo-2-methyl-1H-indol-3-ylmethyl)-N-hydroxyformamide
-
-
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0.000043
GLLI
Homo sapiens
IC50: 0.000043 mM
0.000072
SKI-AC-1
Homo sapiens
IC50: 0.000072 mM, actionin analog
0.000078
SKI-AC-10
Homo sapiens
IC50: 0.000078 mM, actionin analog
0.000076
SKI-AC-11101
Homo sapiens
IC50: 0.000076 mM, actionin analog
-
0.00006
SKI-AC-111101
Homo sapiens
IC50: 0.0000600 mM, actionin analog
0.000427
SKI-AC-111110
Homo sapiens
IC50: 0.000427 mM, actionin analog
-
0.000069
SKI-AC-111111
Homo sapiens
IC50: 0.000069 mM, actionin analog
0.000234
SKI-AC-111112
Homo sapiens
IC50: 0.000234 mM, actionin analog
-
0.000177
SKI-AC-111113
Homo sapiens
IC50: 0.000177 mM, actionin analog
-
0.0003
SKI-AC-111114
Homo sapiens
IC50: 0.000300 mM, actionin analog
-
0.000365
SKI-AC-11112
Homo sapiens
IC50: 0.000365 mM, actionin analog
-
0.0005
SKI-AC-11113
Homo sapiens
IC50: 0.000500 mM, actionin analog
-
0.000276
SKI-AC-11114
Homo sapiens
IC50: 0.000276 mM, actionin analog
-
0.000473
SKI-AC-11115
Homo sapiens
IC50: 0.000473 mM, actionin analog
-
0.000335
SKI-AC-11116
Homo sapiens
IC50: 0.000335 mM, actionin analog
-
0.000086
SKI-AC-11117
Homo sapiens
IC50: 0.000086 mM, actionin analog
0.000115
SKI-AC-11118
Homo sapiens
IC50: 0.000115 mM, actionin analog
0.000134
SKI-AC-11119
Homo sapiens
IC50: 0.000134 mM, actionin analog
-
0.000522
SKI-AC-11128
Homo sapiens
IC50: 0.000522 mM, actionin analog
-
0.0005
SKI-AC-11138
Homo sapiens
IC50: 0.000500 mM, actionin analog
-
0.00006
SKI-AC-11148
Homo sapiens
IC50: 0.0000600 mM, actionin analog
-
0.0005
SKI-AC-11158
Homo sapiens
IC50: 0.000500 mM, actionin analog
-
0.000192
SKI-AC-11168
Homo sapiens
IC50: 0.000192 mM, actionin analog
-
0.0002
SKI-AC-11178
Homo sapiens
IC50: 0.000200 mM, actionin analog
-
0.00012
SKI-AC-11188
Homo sapiens
IC50: 0.000120 mM, actionin analog
0.00009
SKI-AC-11198
Homo sapiens
IC50: 0.000090 mM, actionin analog
0.0005
SKI-AC-3
Homo sapiens
IC50: 0.000500 mM, actionin analog
-
0.0004
SKI-AC-5, SKI-AC-51121
Homo sapiens
IC50: 0.000400 mM, actionin analog
-
0.0004
SKI-AC-51121
Homo sapiens
-
IC50: 0.000400 mM, actionin analog
-
0.000097
SKI-AC-6
Homo sapiens
IC50: 0.000097 mM, actionin analog
0.000093
SKI-AC-8
Homo sapiens
IC50: 0.000093 mM, actionin analog
0.000151
SKI-AC-9
Homo sapiens
IC50: 0.000151 mM, actionin analog
-
0.000404
SKI-AC-I-18
Homo sapiens
IC50: 0.000404 mM, actionin analog
-
0.000239
SKI-AC-I-19
Homo sapiens
IC50: 0.000239 mM, actionin analog
-
0.0041
2',2'-bisepigallocatechin monogallate
Homo sapiens
-
fluorescence polarization assay
0.031
3-methoxycatechol
Homo sapiens
-
fluorescence polarization assay
0.017
7,8-dihydroxyflavone
Homo sapiens
-
fluorescence polarization assay
0.000043 - 0.0055
actinonin
0.048
chloranil
Homo sapiens
-
fluorescence polarization assay
0.038
epigallocatechin 3,5-digallate
Homo sapiens
-
fluorescence polarization assay
0.029
epitheaflavin monogallate
Homo sapiens
-
fluorescence polarization assay
0.012
hematein
Homo sapiens
-
fluorescence polarization assay
0.0027
hematoxylin
Homo sapiens
-
fluorescence polarization assay
0.017
irigenol
Homo sapiens
-
fluorescence polarization assay
0.0088
purpurogallin
Homo sapiens
-
fluorescence polarization assay
0.0057
pyrogallin
Homo sapiens
-
fluorescence polarization assay
0.0089
quinalizarin
Homo sapiens
-
fluorescence polarization assay
0.0061
theaflavin
Homo sapiens
-
fluorescence polarization assay
0.0071
theaflavin monogallate
Homo sapiens
-
fluorescence polarization assay
0.043
thiram
Homo sapiens
-
fluorescamine assay
0.000043
actinonin
Homo sapiens
-
competitive, IC50: 43 nM
0.0055
actinonin
Homo sapiens
-
fluorescence polarization assay
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metabolism
the PDF catalyzed deformylase reaction is part of the methionine molecular cycle, overview
metabolism
-
peptide deformylase (PDF) is a protein of the N-terminal methionine excision pathway that removes formylmethionine from mitochondrial-encoded proteins. PDF is crucial in maintaining mitochondrial function
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
evolution
peptide deformylases constitute a large subfamily of hydrolytic enzymes related to the thermolysin-metzincin HEXXH motif-containing family of metalloproteases. Peptide deformylases are classified into four subtypes based on the structural and sequence similarity of specific conserved domains. All PDFs share a similar three-dimensional structure, are functionally interchangeable in vivo and display similar properties in vitro, indicating that their molecular mechanism has been conserved during evolution. The human mitochondrial enzyme is the only exception as despite its conserved fold it reveals a unique substrate-binding pocket together with an unusual kinetic behaviour, structural basis, overview
evolution
PDFs of all Gram-negative bacteria, some Gram-positive bacteria, and all eukaryotes fall systematically into type I class. The type II PDFs are found in Gram-positive bacteria (with low C+G content) and mycoplasma
malfunction
inhibition of the MEK/ERK, but not PI3K or mTOR, pathway reduces the expression of the enzyme in both colon and lung cancer cell lines
malfunction
a decrease in human cell growth results from PDF inhibitors actinonin and its analogues
physiological function
the enzyme is essential and involved in the essential removal of the formyl group from the N-terminal methionine during the early phase of protein translation, barely after the nascent chain has emerged from the ribosome
physiological function
the MEK/ERK pathway plays a role in regulating the expression of the peptide deformylase in human tissues, overview. The enzyme may act as an oncogene to promote cancer cell proliferation
physiological function
peptide deformylase (PDF) is a metalloenzyme and responsible for catalyzing the removal of the N-formyl group from N-terminal methionine following translation. Removal of the formyl group from polypeptide by PDF is a necessary activity for prokaryotic cell viability. This activity is not believed to be important in eukaryotic cells until recently, because nuclear encoded proteins are not N-formylated. But in eukaryotes, mitochondrial protein synthesis may also involve the formylation and deformylation process. The mitochondrial localization of HsPDF, and N-formylation of human mitochondrial translation products for translation initiation point at the 13 proteins encoded by the mitochondrial genome as putative substrates of HsPDF
additional information
enzyme structure comparison to plant enzyme from Arabidopsis thaliana, overview. A cysteine residue is involved in metal coordination within the active site, together with the two histidines from the thermolysin-metzincin HEXXH motif. The natural product tripeptide Met-Ala-Ser does not change the unfolding process of the protein, binding structure of the peptide to the enzyme, overview
additional information
-
enzyme structure comparison to plant enzyme from Arabidopsis thaliana, overview. A cysteine residue is involved in metal coordination within the active site, together with the two histidines from the thermolysin-metzincin HEXXH motif. The natural product tripeptide Met-Ala-Ser does not change the unfolding process of the protein, binding structure of the peptide to the enzyme, overview
additional information
proposed molecular catalytic mechanism of PDF, overview. The active site of PDF proteins contains three substrate binding pockets along with the metal binding site. These pockets are referred to as S1', S2', and S3' pockets and corresponding positions on substrate or inhibitors are referred to as P1', P2', and P3'
additional information
-
proposed molecular catalytic mechanism of PDF, overview. The active site of PDF proteins contains three substrate binding pockets along with the metal binding site. These pockets are referred to as S1', S2', and S3' pockets and corresponding positions on substrate or inhibitors are referred to as P1', P2', and P3'
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Lee, M.D.; Antczak, C.; Li, Y.; Sirotnak, F.M.; Bornmann, W.G.; Scheinberg, D.A.
A new human peptide deformylase inhibitable by actinonin
Biochem. Biophys. Res. Commun.
312
309-315
2003
Homo sapiens
brenda
Nguyen, K.T.; Hu, X.; Colton, C.; Chakrabarti, R.; Zhu, M.X.; Pei, D.
Characterization of a human peptide deformylase: implications for antibacterial drug design
Biochemistry
42
9952-9958
2003
Escherichia coli, Homo sapiens
brenda
Lee, M.D.; She, Y.; Soskis, M.J.; Borella, C.P.; Gardner, J.R.; Hayes, P.A.; Dy, B.M.; Heaney, M.L.; Philips, M.R.; Bornmann, W.G.; Sirotnak, F.M.; Scheinberg, D.A.
Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics
J. Clin. Invest.
114
1107-1116
2004
Homo sapiens (Q9HBH1), Homo sapiens
brenda
Antczak, C.; Shum, D.; Escobar, S.; Bassit, B.; Kim, E.; Seshan, V.E.; Wu, N.; Yang, G.; Ouerfelli, O.; Li, Y.M.; Scheinberg, D.A.; Djaballah, H.
High-throughput identification of inhibitors of human mitochondrial peptide deformylase
J. Biomol. Screen.
12
521-535
2007
Homo sapiens
brenda
Boularot, A.; Giglione, C.; Petit, S.; Duroc, Y.; Alves de Sousa, R.; Larue, V.; Cresteil, T.; Dardel, F.; Artaud, I.; Meinnel, T.
Discovery and refinement of a new structural class of potent peptide deformylase inhibitors
J. Med. Chem.
50
10-20
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q9FUZ2), Arabidopsis thaliana (Q9FV53), Bacillus subtilis, Escherichia coli, Homo sapiens
brenda
Escobar-Alvarez, S.; Goldgur, Y.; Yang, G.; Ouerfelli, O.; Li, Y.; Scheinberg, D.A.
Structure and activity of human mitochondrial peptide deformylase, a novel cancer target
J. Mol. Biol.
387
1211-1228
2009
Homo sapiens (Q9HBH1), Homo sapiens
brenda
Sharma, A.; Khuller, G.K.; Sharma, S.
Peptide deformylase--a promising therapeutic target for tuberculosis and antibacterial drug discovery
Expert Opin. Ther. Targets
13
753-765
2009
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
brenda
Chikhi, A.; Bensegueni, A.
In silico study of the selective inhibition of bacterial peptide deformylases by several drugs
J. Proteomics Bioinform.
3
61-65
2010
Escherichia coli (P0A6K3), Bacillus cereus (Q819K2), Arabidopsis thaliana (Q9FUZ2), Homo sapiens (Q9HBH1)
-
brenda
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
Protein Expr. Purif.
70
224-230
2010
Homo sapiens
brenda
Pereira-Castro, I.; Costa, L.T.; Amorim, A.; Azevedo, L.
Transcriptional regulation of the human mitochondrial peptide deformylase (PDF)
Biochem. Biophys. Res. Commun.
421
825-831
2012
Homo sapiens
brenda
Fieulaine, S.; Desmadril, M.; Meinnel, T.; Giglione, C.
Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart
Acta Crystallogr. Sect. D
70
242-252
2014
Homo sapiens (Q9HBH1), Homo sapiens
brenda
Randhawa, H.; Chikara, S.; Gehring, D.; Yildirim, T.; Menon, J.; Reindl, K.M.
Overexpression of peptide deformylase in breast, colon, and lung cancers
BMC Cancer
13
321
2013
Homo sapiens (Q9HBH1), Homo sapiens
brenda
Sangshetti, J.; Khan, F.; Shinde, D.
Peptide deformylase a new target in antibacterial, antimalarial and anticancer drug discovery
Curr. Med. Chem.
22
214-236
2015
Bacillus subtilis (P94462), Bacillus subtilis 168 (P94462), Escherichia coli (P0A6K3), Haemophilus influenzae (P44786), Haemophilus influenzae ATCC 51907 (P44786), Haemophilus influenzae DSM 11121 (P44786), Haemophilus influenzae KW20 (P44786), Haemophilus influenzae RD (P44786), Helicobacter pylori (P56419), Helicobacter pylori 26695 (P56419), Helicobacter pylori ATCC 700392 (P56419), Homo sapiens (Q9HBH1), Homo sapiens, Mycobacterium tuberculosis (P9WIJ3), Mycobacterium tuberculosis ATCC 25618 (P9WIJ3), Mycobacterium tuberculosis H37Rv (P9WIJ3), Plasmodium falciparum (Q8I372), Plasmodium falciparum isolate 3D7 (Q8I372), Staphylococcus aureus (P68826)
brenda
Gao, J.; Wang, T.; Qiu, S.; Zhu, Y.; Liang, L.; Zheng, Y.
Structure-based drug design of small molecule peptide deformylase inhibitors to treat cancer
Molecules
21
396
2016
Homo sapiens (Q9HBH1), Homo sapiens
brenda