Unknown

Dataset Information

0

Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls.


ABSTRACT: The major constituent of bacterial cell walls is peptidoglycan, which, in its crosslinked form, is a polymer of considerable complexity that encases the entire bacterium. A functional cell wall is indispensable for survival of the organism. There are several dozen enzymes that assemble and disassemble the peptidoglycan dynamically within each bacterial generation. Understanding of the nature of these transformations is critical knowledge for these events. Octasaccharide peptidoglycans were prepared and studied with seven recombinant cell-wall-active enzymes (SltB1, MltB, RlpA, mutanolysin, AmpDh2, AmpDh3, and PBP5). With the use of highly sensitive mass spectrometry methods, we described the breadth of reactions that these enzymes catalyzed with peptidoglycan and shed light on the nature of the cell wall alteration performed by these enzymes. The enzymes exhibit broadly distinct preferences for their substrate peptidoglycans in the reactions that they catalyze.

SUBMITTER: Lee M 

PROVIDER: S-EPMC5681705 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls.

Lee Mijoon M   Hesek Dusan D   Lastochkin Elena E   Dik David A DA   Boggess Bill B   Mobashery Shahriar S  

Chembiochem : a European journal of chemical biology 20170725 17


The major constituent of bacterial cell walls is peptidoglycan, which, in its crosslinked form, is a polymer of considerable complexity that encases the entire bacterium. A functional cell wall is indispensable for survival of the organism. There are several dozen enzymes that assemble and disassemble the peptidoglycan dynamically within each bacterial generation. Understanding of the nature of these transformations is critical knowledge for these events. Octasaccharide peptidoglycans were prepa  ...[more]

Similar Datasets

| S-EPMC4432689 | biostudies-literature
| S-EPMC3382501 | biostudies-other
| S-EPMC4000856 | biostudies-other
| S-EPMC1206819 | biostudies-other
| S-EPMC3477100 | biostudies-literature
| S-EPMC4333057 | biostudies-other
| S-EPMC5864212 | biostudies-literature
| S-EPMC3148234 | biostudies-literature
| S-EPMC1177711 | biostudies-other
2017-08-16 | GSE102664 | GEO