A weak dd-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli
FEMS Microbiology Letters, ISSN: 0378-1097, Vol: 303, Issue: 1, Page: 76-83
2010
- 26Citations
- 31Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations26
- Citation Indexes26
- 26
- CrossRef25
- Captures31
- Readers31
- 31
Article Description
Penicillin-binding protein (PBP) 5 plays a critical role in maintaining normal cellular morphology in mutants of Escherichia coli lacking multiple PBPs. The most closely related homologue, PBP 6, is 65% identical to PBP 5, but is unable to substitute for PBP 5 in returning these mutants to their wild-type shape. The relevant differences between PBPs 5 and 6 are localized in a 20-amino acid stretch of domain I in these proteins, which includes the canonical KTG motif at the active site. We determined how these differences affected the enzymatic properties of PBPs 5 and 6 toward β-lactam binding and the binding and hydrolysis of two peptide substrates. We also investigated the enzymatic properties of recombinant fusion proteins in which active site segments were swapped between PBPs 5 and 6. The results suggest that the in vivo physiological role of PBP 5 is distinguished from PBP 6 by the higher degree of dd-carboxypeptidase activity of the former. © 2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=74349093311&origin=inward; http://dx.doi.org/10.1111/j.1574-6968.2009.01863.x; http://www.ncbi.nlm.nih.gov/pubmed/20015336; https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.2009.01863.x; https://dx.doi.org/10.1111/j.1574-6968.2009.01863.x; https://academic.oup.com/femsle/article/303/1/76/559805
Oxford University Press (OUP)
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