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Information on EC 3.5.1.88 - peptide deformylase and Organism(s) Thermotoga maritima and UniProt Accession P96113

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.88 peptide deformylase
IUBMB 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).
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This record set is specific for:
Thermotoga maritima
UNIPROT: P96113
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
Synonyms
peptide deformylase, hspdf, pdf-1, polypeptide deformylase, pdf1a, hppdf, pdf1b, pdf-2, vp16 pdf, tbpdf1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deformylase, peptide N-formylmethionine
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hydrolase, aminoacyl-transfer ribonucleate
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PDF
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Polypeptide deformylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amide bond
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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 hide
369636-51-1
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37289-08-0
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9032-86-4
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9054-98-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-formyl-L-methionine-polypeptide + H2O
formate + L-methionine-polypeptide
show the reaction diagram
involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-formyl-L-methionine-polypeptide + H2O
formate + L-methionine-polypeptide
show the reaction diagram
involved in polypeptide synthesis by removal of the formyl-group from methionine in growing polypeptides
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
can replace Fe2+ without loss of activity, enhances stability
Fe2+
required, irreversible oxidation to Fe3+ results in almost complete loss of activity
Ni2+
can replace Fe2+ without loss of activity, enhances stability
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
instable towards oxidation due to the oxidation of the metal ligating cysteine residue
666015
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme using His-tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
potential target or the development of new antibacterial agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mazel, D.; Coic, E.; Blanchard, S.; Saurin, W.; Marliere, P.
A survey of polypeptide deformylase function throughout the eubacterial lineage
J. Mol. Biol.
266
939-949
1997
Bacillus subtilis, Calothrix sp., Lactococcus lactis, Thermotoga maritima
Manually annotated by BRENDA team
Kreusch, A.; Spraggon, G.; Lee, C.C.; Klock, H.; McMullan, D.; Ng, K.; Shin, T.; Vincent, J.; Warner, I.; Ericson, C.; Lesley, S.A.
Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase
J. Mol. Biol.
330
309-321
2003
Escherichia coli (P0A6K3), Escherichia coli, Plasmodium falciparum, Pseudomonas aeruginosa (Q9I7A8), Pseudomonas aeruginosa, Staphylococcus aureus (P68826), Staphylococcus aureus, Staphylococcus aureus ATCC 2913 (P68826), Streptococcus pneumoniae (Q9F2F0), Streptococcus pneumoniae, Thermotoga maritima (P96113), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (P96113)
Manually annotated by BRENDA team