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PMID:7896716

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Contents

Citation

Meinnel, T and Blanquet, S (1995) Enzymatic properties of Escherichia coli peptide deformylase. J. Bacteriol. 177:1883-7

Abstract

Since its discovery in crude extracts in the late sixties, Escherichia coli peptide deformylase activity could not be further characterized because of an apparent extreme instability. We show that this behavior was caused by an inadequate activity assay, involving substrate concentration inhibition and substrate precipitation in crude extracts. The homogeneous protein, as it was previously purified (T. Meinnel and S. Blanquet J. Bacteriol. 175:7737-7740, 1993), had actually retained its initial activity. The influence on the deformylation reaction of several factors was studied and used to improve the activity assay. Pure peptide deformylase proves to act only on peptide substrates with an N-formylmethionyl moiety. In agreement with the occurrence of zinc in the enzyme, peptide deformylase activity is inhibited by 1,10-phenanthroline.

Links

PubMed PMC176821

Keywords

Amidohydrolases; Amino Acid Sequence; Aminopeptidases/antagonists & inhibitors; Aminopeptidases/isolation & purification; Aminopeptidases/metabolism; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Molecular Sequence Data; Zinc/analysis

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Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status

def:Gene_Product(s)

GO:0042586

peptide deformylase activity

IDA: Inferred from Direct Assay

F

complete

def:Gene_Product(s)

GO:0008270

zinc ion binding

IDA: Inferred from Direct Assay

F

complete

def:Gene_Product(s)

GO:0016787

hydrolase activity

IDA: Inferred from Direct Assay

F

complete

def:Gene_Product(s)

GO:0031365

N-terminal protein amino acid modification

IDA: Inferred from Direct Assay

P

complete

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