Evolution of Enzymatic Activities in the Enolase Superfamily:  Functional Assignment of Unknown Proteins in <i>Bacillus subtilis </i>and <i>Escherichia coli</i> as <scp>l</scp>-Ala-<scp>d</scp>/<scp>l</scp>-Glu Epimerases

Schmidt, Dawn M. Z.; Hubbard, Brian K.; Gerlt, J.A.

doi:10.1021/bi011640x

Cited by 79 publications

(92 citation statements)

References 21 publications

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“…The E. coli MpaA amidase removes the meso-DAP from L-Ala-D-Glu [184]. E. coli YcjG epimerizes D-Glu to L-Glu forming L-Ala-L-Glu, which is hydrolysed to individual amino acids by PepD [185,186]. This pathway of amino acid degradation has not been studied in P. aeruginosa and bioinformatics analyses of the protein sequences of MpaA, YcjG and PepD shows the absence of these in the P. aeruginosa PAO1 strain.…”

Section: Convergence Of Recycling and Biosynthesismentioning

confidence: 99%

Cell-wall recycling and synthesis in Escherichia coli and Pseudomonas aeruginosa – their role in the development of resistance

Dhar

Kumari

Balasubramanian

et al. 2018

Journal of Medical Microbiology

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The bacterial cell-wall that forms a protective layer over the inner membrane is called the murein sacculus -a tightly crosslinked peptidoglycan mesh unique to bacteria. Cell-wall synthesis and recycling are critical cellular processes essential for cell growth, elongation and division. Both de novo synthesis and recycling involve an array of enzymes across all cellular compartments, namely the outer membrane, periplasm, inner membrane and cytoplasm. Due to the exclusivity of peptidoglycan in the bacterial cell-wall, these players are the target of choice for many antibacterial agents. Our current understanding of cell-wall biochemistry and biogenesis in Gram-negative organisms stems mostly from studies of Escherichia coli. An incomplete knowledge on these processes exists for the opportunistic Gram-negative pathogen, Pseudomonas aeruginosa. In this review, cell-wall synthesis and recycling in the various cellular compartments are compared and contrasted between E. coli and P. aeruginosa. Despite the fact that there is a remarkable similarity of these processes between the two bacterial species, crucial differences alter their resistance to b-lactams, fluoroquinolones and aminoglycosides. One of the common mediators underlying resistance is the amp system whose mechanism of action is closely associated with the cell-wall recycling pathway. The activation of amp genes results in expression of AmpC blactamase through its cognate regulator AmpR which further regulates multi-drug resistance. In addition, other cell-wall recycling enzymes also contribute to antibiotic resistance. This comprehensive summary of the information should spawn new ideas on how to effectively target cell-wall processes to combat the growing resistance to existing antibiotics.

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Section: Convergence Of Recycling and Biosynthesismentioning

confidence: 99%

Cell-wall recycling and synthesis in Escherichia coli and Pseudomonas aeruginosa – their role in the development of resistance

Dhar

Kumari

Balasubramanian

et al. 2018

Journal of Medical Microbiology

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show abstract

“…More information on the substrate specificity of MpaA and on a possible requirement for zinc awaits overproduction and purification of the enzyme. (105). L-Ala-L-Glu is a substrate for PepD, a dipeptidase of E. coli with a broad specificity (107).…”

Section: Mpaa: ␥-D-glutamyl-meso-diaminopimelate Amidasementioning

confidence: 99%

How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan)

Park

Uehara

2008

Microbiol Mol Biol Rev

381

498

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SUMMARY The phenomenon of peptidoglycan recycling is reviewed. Gram-negative bacteria such as Escherichia coli break down and reuse over 60% of the peptidoglycan of their side wall each generation. Recycling of newly made peptidoglycan during septum synthesis occurs at an even faster rate. Nine enzymes, one permease, and one periplasmic binding protein in E. coli that appear to have as their sole function the recovery of degradation products from peptidoglycan, thereby making them available for the cell to resynthesize more peptidoglycan or to use as an energy source, have been identified. It is shown that all of the amino acids and amino sugars of peptidoglycan are recycled. The discovery and properties of the individual proteins and the pathways involved are presented. In addition, the possible role of various peptidoglycan degradation products in the induction of β-lactamase is discussed.

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“…The search for members of the enolase superfamily in the E. coli and B. subtilis genomes led to the discovery of the L-alanyl-D/L-glutamate epimerases YcjG and YkfB, respectively, which convert L-Ala-D-Glu to L-Ala-L-Glu (233). Their crystal structures (Fig.…”

Section: Penicillin-insensitive Peptidasesmentioning

confidence: 99%

Peptidoglycan Hydrolases of Escherichia coli

Heijenoort

2011

Microbiol Mol Biol Rev

187

233

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SUMMARY The review summarizes the abundant information on the 35 identified peptidoglycan (PG) hydrolases of Escherichia coli classified into 12 distinct families, including mainly glycosidases, peptidases, and amidases. An attempt is also made to critically assess their functions in PG maturation, turnover, elongation, septation, and recycling as well as in cell autolysis. There is at least one hydrolytic activity for each bond linking PG components, and most hydrolase genes were identified. Few hydrolases appear to be individually essential. The crystal structures and reaction mechanisms of certain hydrolases having defined functions were investigated. However, our knowledge of the biochemical properties of most hydrolases still remains fragmentary, and that of their cellular functions remains elusive. Owing to redundancy, PG hydrolases far outnumber the enzymes of PG biosynthesis. The presence of the two sets of enzymes acting on the PG bonds raises the question of their functional correlations. It is difficult to understand why E. coli keeps such a large set of PG hydrolases. The subtle differences in substrate specificities between the isoenzymes of each family certainly reflect a variety of as-yet-unidentified physiological functions. Their study will be a far more difficult challenge than that of the steps of the PG biosynthesis pathway.

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Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as l-Ala-d/l-Glu Epimerases

Cited by 79 publications

References 21 publications

Cell-wall recycling and synthesis in Escherichia coli and Pseudomonas aeruginosa – their role in the development of resistance

Cell-wall recycling and synthesis in Escherichia coli and Pseudomonas aeruginosa – their role in the development of resistance

How Bacteria Consume Their Own Exoskeletons (Turnover and Recycling of Cell Wall Peptidoglycan)

Peptidoglycan Hydrolases of Escherichia coli

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