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  Peptide deformylase

Becker, A., & Kabsch, W. (2001). Peptide deformylase. In A. Messerschmidt, R. Huber, & T. W. Poulos K. (Eds.), Handbook of Metalloproteins (pp. 915-928). Chichester: Interscience Wiley. doi:10.1002/0470028637.met165.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-E408-7 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-E409-5
Genre: Book Chapter
Alternative Title : Peptide deformylase

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HdbkMetalloprot_2001_915.pdf (Any fulltext), 441KB
 
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http://onlinelibrary.wiley.com/doi/10.1002/0470028637.met165/pdf (Any fulltext)
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 Creators:
Becker, Andreas1, Author           
Kabsch, Wolfgang1, 2, Author           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: mononuclear iron peptide hydrolase; transformylase property; methionyl t-RNA formyltransferase; eubacterial protein synthesis
 Abstract: Peptide deformylase (EC 3.5.1.31) is a mononuclear iron enzyme that cleaves the formyl group of the N-terminal formyl-methionine residue of nascent polypeptide chains in eubacteria. It is strictly stereospecific for a l-amino acid as the first residue of formyl-peptide substrates and strongly prefers substrates with at least two or more residues. The native enzyme from Escherichia coli is a monomeric protein of 168 amino acid residues that contains one tightly bound Fe2+ ion. The metal ion is tetrahedrally coordinated by a water molecule and the side chains of residues Cys90, His132, and His136. Similar to thermolysin, the two histidines are part of the HEXXH motif and the glutamate residue is required for enzymatic activity. The native iron form of peptide deformylase is extremely sensitive to oxidative destruction. On substitution of the iron ion by Ni2+ or Co2+ the enzyme is insensitive to oxidation and maintains its activity, whereas the Zn2+ form is nearly inactive.

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Language(s): eng - English
 Dates: 2006-04-152001
 Publication Status: Issued
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Internal
 Identifiers: eDoc: 666193
Other: 5046
URI: http://onlinelibrary.wiley.com/doi/10.1002/0470028637.met165/abstract
URI: http://onlinelibrary.wiley.com/doi/10.1002/0470028637.met165/full
DOI: 10.1002/0470028637.met165
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Title: Handbook of Metalloproteins
Source Genre: Book
 Creator(s):
Messerschmidt, A., Author
Huber, R., Author
Poulos K., T.: Wieghardt, Author
Messerschmidt, A., Editor
Huber, R., Editor
Poulos K., T.: Wieghardt, Editor
Affiliations:
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Publ. Info: Chichester : Interscience Wiley
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 915 - 928 Identifier: ISBN: 0-471-62743-7