An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway (Q24297180)

Methionyl aminopeptidase type 1D, mitochondrial

GOA release 2020-03-11

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N-terminal protein amino acid modification

GOA release 2020-03-11

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GOA release 2020-03-11

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5

Thierry Meinnel

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Carmela Giglione

object named as

Carmela Giglione

2

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author name string

Alexandre Serero

1

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Alessandro Sardini

3

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Juan Martinez-Sanz

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

26 December 2003

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published in

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volume

278

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issue

52

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page(s)

52953-63

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cites work

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Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor

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Enzymatic properties of Escherichia coli peptide deformylase

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Control of peptide deformylase activity by metal cations.

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The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents

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Solution structure of nickel-peptide deformylase

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Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins.

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Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal

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The C-terminal domain of peptide deformylase is disordered and dispensable for activity

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Identifiers

DOI

10.1074/JBC.M309770200

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Consolidated OpenCitations Corpus – April 2017

2894199

2894199

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference