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Information on EC 3.5.1.88 - peptide deformylase and Organism(s) Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai and UniProt Accession Q93LE9

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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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Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai
UNIPROT: Q93LE9
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Word Map
The enzyme appears in selected viruses and cellular organisms
Synonyms
peptide deformylase, hspdf, pdf-1, polypeptide deformylase, hppdf, pdf1a, 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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