| Transpeptidase-mediated incorporation of D-amino acids into bacterial peptidoglycan. | |
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MedLine Citation:
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PMID: 21682301 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The β-lactams are the most important class of antibiotics in clinical use. Their lethal targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the cross-linking of bacterial peptidoglycan (PG) during cell wall synthesis. The transpeptidation reaction occurs in two steps, the first being formation of a covalent enzyme intermediate and the second involving attack of an amine on this intermediate. Here we use defined PG substrates to dissect the individual steps catalyzed by a purified E. coli transpeptidase. We demonstrate that this transpeptidase accepts a set of structurally diverse D-amino acid substrates and incorporates them into PG fragments. These results provide new information on donor and acceptor requirements as well as a mechanistic basis for previous observations that noncanonical D-amino acids can be introduced into the bacterial cell wall. |
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Authors:
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Tania J Lupoli; Hirokazu Tsukamoto; Emma H Doud; Tsung-Shing Andrew Wang; Suzanne Walker; Daniel Kahne |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-06-27 |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: 133 ISSN: 1520-5126 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2011 Jul |
Date Detail:
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Created Date: 2011-07-13 Completed Date: 2011-11-03 Revised Date: 2012-04-27 |
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: 10748-51 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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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Amino Acids / chemistry*, metabolism* Escherichia coli / enzymology, metabolism* Peptidoglycan / metabolism* Peptidyl Transferases / chemistry, metabolism* Stereoisomerism |
| Grant Support | |
ID/Acronym/Agency:
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R01 GM066174/GM/NIGMS NIH HHS; R01 GM066174/GM/NIGMS NIH HHS; R01 GM066174-10/GM/NIGMS NIH HHS; R01 GM066174-11/GM/NIGMS NIH HHS; R01 GM076710/GM/NIGMS NIH HHS; R01 GM076710-04/GM/NIGMS NIH HHS; R01 GM076710-06/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Peptidoglycan; EC 2.3.2.12/Peptidyl Transferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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