Any feedback?
Information on EC 3.5.1.88 - peptide deformylase and Organism(s) Homo sapiens and UniProt Accession Q9HBH1
for references in articles please use BRENDA:EC3.5.1.88Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.1.88 peptide deformylaseIUBMB Comments
Requires Fe(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.31 (formylmethionine deformylase).
Specify your search results
Word Map
- 3.5.1.88
- actinonin
- medicine
-
n-formylated
-
deformylation
- eubacteria
-
hydroxamic
- drug development
-
formyltransferase
-
oxazolidinone
- catarrhalis
- linezolid
- moraxella
-
hexxh
- biotechnology
- synthesis
- agriculture
- molecular biology
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
peptide deformylase, hspdf, pdf-1, polypeptide deformylase, pdf1a, hppdf, pdf1b, pdf-2, atdef2, vp16 pdf, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deformylase, peptide N-formylmethionine
-
-
-
-
hydrolase, aminoacyl-transfer ribonucleate
-
-
-
-
PDF
Polypeptide deformylase
-
-
-
-
PDF
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amide bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
formyl-L-methionyl peptide amidohydrolase
Requires Fe(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.31 (formylmethionine deformylase).
CAS REGISTRY NUMBER
COMMENTARY
369636-51-1
-
37289-08-0
-
9032-86-4
-
9054-98-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formyl-MAHA + H2O
formate + MAHA
peptide substrate derived from mitochondrial cytochrome c oxidase subunit II
-
-
?
formyl-MFAD + H2O
formate + MFAD
peptide substrate derived from mitochondrial cytochrome c oxidase subunit I
-
-
?
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-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-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-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
-
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-formyl-L-methionine polypeptide + H2O
formate + methionine-polypeptide
-
-
-
-
?
N-formyl-L-methionine-polypeptide + H2O
formate + L-methionine-polypeptide
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Co2+
Fe2+
-
only Fe2+ and Co2+ ions are capable of supporting the enzyme activity of PDF
additional information
Co2+
-
Co2+ is an optimal metal for increasing the activity of purified thioredoxin-fused PDF
additional information
the metal ion in the active site of PDF is tetrahedrally ligated and bound to the two histidines from the HEPhiDH motif, as well to a cysteine and a water molecule
additional information
-
the metal ion in the active site of PDF is tetrahedrally ligated and bound to the two histidines from the HEPhiDH motif, as well to a cysteine and a water molecule
additional information
-
Zn2+ and Ni2+ are not capable of supporting the enzyme activity of PDF
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-N4-hydroxy-N1-[(2S)-3-methyl-1-oxo-1-(piperidin-1-yl)butan-2-yl]-2-pentylbutanediamide
-
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-[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
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
-
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
-
(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
-
-
N-(1-benzenesulfonyl-5-bromo-2-methyl-1H-indol-3-ylmethyl)-N-hydroxyformamide
-
-
actinonin
enzyme inhibitor, inhibits the growth of both cancer and non-cancer cell lines
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00015
(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
-
-
0.2
N-(1-benzenesulfonyl-5-bromo-2-methyl-1H-indol-3-ylmethyl)-N-hydroxyformamide
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
expression pattern of the enzyme in cancerous tissues, overview
additional information
-
expression pattern of the enzyme in cancerous tissues, overview
additional information
various types of cancer cell lines from breast, colon, kidney, liver, lung, ovarian, prostate, or thyroid. The enzyme levels are elevated in cancer cell lines compared to non-cancer lines, PDF mRNA levels are significantly increased in breast, colon, and lung cancer samples
additional information
-
various types of cancer cell lines from breast, colon, kidney, liver, lung, ovarian, prostate, or thyroid. The enzyme levels are elevated in cancer cell lines compared to non-cancer lines, PDF mRNA levels are significantly increased in breast, colon, and lung cancer samples
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
the PDF catalyzed deformylase reaction is part of the methionine molecular cycle, overview
physiological function
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
additional information
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'
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DEFM_HUMAN
243
0
27013
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
comparison of PDF structures from Escherichia coli (PDB ID 1BS7), Staphylococcus aureus (PDB ID 2AI9), Plasmodium falciparum (PBD ID 1BS8), and Homo sapiens (PBD ID 3G5K), overview. Detailed analysis of the three-dimensional structure of human PDF with bound Co2+
additional information
-
comparison of PDF structures from Escherichia coli (PDB ID 1BS7), Staphylococcus aureus (PDB ID 2AI9), Plasmodium falciparum (PBD ID 1BS8), and Homo sapiens (PBD ID 3G5K), overview. Detailed analysis of the three-dimensional structure of human PDF with bound Co2+
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His6-tagged truncated enzyme free or complexed with inhibitor actinonin or natural product peptide Met-Ala-Ser, PEG 5000 MME or PEG 6000 are employed as a precipitant, crystallization with or without 15 mM actinonin, free crystal soaking in 10 mM Met-Ala-Ser, usage of 15% PEG 5000 MME or PEG 6000, 100 mM MES buffer pH 5.5, 20% glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution, molecular replacement
the structures of peptide deformylase and of peptide deformylase in complex with actinonin are determined at 1.7 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C50G/E115L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E115L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E173L
-
the ratio of turnover number to Km-value for the substrate formyl-Met-Leu-p-nitroanilide is increased 3.7fold. The ratio of turnover number to Km-value for the substrate formyl-Met-Ala-His-Ala-Ala-Gln is increased 3.5fold. The ratio of turnover number to Km-value for the substrate formyl-Met-ThrGln-Ser-His is increased 1.5fold. The ratio of turnover number to Km-value for the substrate formyl-Met-Thr-Met-His-Thr-Thr is increased 2.4fold
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by chromatography on a Ni2+ Sepharose high-performance column, gel filtration and ammonium sulfate precipitation
recombinant C-terminally His6-tagged truncated enzyme by nickel affinity and anion exchange chromatography, followed by gel filtration and ultrafiltration to homogeneity
glutathione Sepharose column chromatography and Ni Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated HsPDF lacking the first 63 amino acids, which correspond to the mitochondrial targeting sequence, is cloned into the vector pET-15b for expression in Escherichia coli BL21DE3 pLys cells
sequence comparison, recombinant expression of C-terminally His6-tagged human-like PDF protein, composed of 197 residues
GST-tagged original PDF protein and thioredoxin-tagged original PDF are expressed in both Escherichia coli BL21 (DE3) and Rosetta (DE3) strains, respectively
-
truncated form that lacks the N-terminal 58-amino-acid targeting sequence is overexpressed in Escherichia coli as a Co2+-substituted protein, is catalytically active in deformylating N-formylated peptides. Expression of HsPDF fused to the enhanced green fluorescence protein in human embryonic kidney cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
enzyme expression is regulated by members of the Sp family of transcription factors, particularly by Sp1
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
human peptide deformylase (HsPDF) is an important target for anticancer drug discovery
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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)
-
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
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
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
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
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)
EXTERNAL LINKS (specific for EC-Number 3.5.1.88)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
