| Studying a cell division amidase using defined peptidoglycan substrates. | |
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MedLine Citation:
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PMID: 19957935 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Three periplasmic N-acetylmuramoyl-l-alanine amidases are critical for hydrolysis of septal peptidoglycan, which enables cell separation. The amidases cleave the amide bond between the lactyl group of muramic acid and the amino group of l-alanine to release a peptide moiety. Cell division amidases remain largely uncharacterized because substrates suitable for studying them have not been available. Here we have used synthetic peptidoglycan fragments of defined composition to characterize the catalytic activity and substrate specificity of the important Escherichia coli cell division amidase AmiA. We show that AmiA is a zinc metalloprotease that requires at least a tetrasaccharide glycopeptide substrate for cleavage. The approach outlined here can be applied to many other cell wall hydrolases and should enable more detailed studies of accessory proteins proposed to regulate amidase activity in cells. |
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Authors:
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Tania J Lupoli; Tohru Taniguchi; Tsung-Shing Wang; Deborah L Perlstein; Suzanne Walker; Daniel E Kahne |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: 131 ISSN: 1520-5126 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2009 Dec |
Date Detail:
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Created Date: 2009-12-23 Completed Date: 2010-03-02 Revised Date: 2011-05-02 |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: United States |
Other Details:
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Languages: eng Pagination: 18230-1 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amidohydrolases
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chemistry,
metabolism* Catalysis Cell Division* Escherichia coli / cytology, enzymology Escherichia coli Proteins Metalloendopeptidases Peptide Fragments / chemistry, metabolism* Peptidoglycan / chemistry, metabolism* Substrate Specificity Zinc |
| Grant Support | |
ID/Acronym/Agency:
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GM007598/GM/NIGMS NIH HHS; GM066174/GM/NIGMS NIH HHS; GM076710/GM/NIGMS NIH HHS; R01 GM066174-08/GM/NIGMS NIH HHS; R01 GM066174-10/GM/NIGMS NIH HHS; R01 GM076710-04/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Escherichia coli Proteins; 0/Peptide Fragments; 0/Peptidoglycan; 7440-66-6/Zinc; EC 3.4.24.-/Metalloendopeptidases; EC 3.5.-/Amidohydrolases; EC 3.5.1.4/amidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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