Scission of the Lactyl Ether Bond of N-Acetylmuramic Acid by Escherichia coli “Etherase”

Jaeger, Tina; Arsic, Momo; Mayer, Christoph

doi:10.1074/jbc.m502208200

Cited by 50 publications

(87 citation statements)

References 31 publications

(32 reference statements)

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“…2A and B, lanes 2 and 3), confirming the prediction that MurNAc-6-phosphate is the inducer of MurR. 8) As expected from this hypothesis, and in agreement with previous observations, 4) this induction was, however, not observed with GalNAc and GalN ( Fig. 2A and B, lanes 4 and 5).…”

supporting

confidence: 80%

“…10) However, high-level expression of the murQP operon is needed for growth on MurNAc as the sole source of carbon and energy. 8,11) On the other hand, in rich media, the murPQ operon must be repressed tightly to avoid degradation of cell walls. It is thus plausible that under nutrient-rich conditions, murR is highly expressed to maintain a high level of MurR repressor.…”

mentioning

confidence: 99%

“…9) MurNAc, a component of the bacterial cell wall, can be used as a carbon source after conversion to GluNAc by a combination of MurP (MurNAc-specific PTS enzyme) and MurQ (MurNAc-6-P etherase). 8) To utilize MurNAc as a carbon source, CRP, activated by cAMP when glucose is low, activates the murQP operon, 4) as in the case of the utilization of other non-glucose sugars. A low-level of the murQP operon is sufficient for the degradation of the cell wall.…”

mentioning

confidence: 99%

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Two Modes of Autoregulation of themurRRepressor inEscherichia coli

Ishihama

2009

Bioscience, Biotechnology, and Biochemistry

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The murPQ operon of Escherichia coli encoding the enzymes for degradation of MurNAc is derepressed by MurR (YfeT) in the presence of MurNAc-6-phosphate. MurR also represses its own expression. We found that murR is stimulated in rich medium. This activation involves MurR and most of the IIBC components of the phosphotransferase system, suggesting auto-induction of murR by an activated form of MurR.

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confidence: 80%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Two Modes of Autoregulation of themurRRepressor inEscherichia coli

Ishihama

2009

Bioscience, Biotechnology, and Biochemistry

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“…Besides recycling its own PG, E. coli is able to grow on PG fragments, GlcNAc, and MurNAc as the sole carbon and nitrogen sources (118,197,306). Presumably, hydrolases of the recycling process, together with other cell enzymes, have an important role in the uptake and use of these exogenous products as metabolic fuel.…”

Section: Hydrolases and Peptidoglycan Recyclingmentioning

confidence: 99%

“…Interestingly, the yfeW gene encoding PBP4b is in an operon together with the murP and murQ genes, which are required for growth on MurNAc (118). DD-Carboxypeptidase PBP5.…”

Section: Penicillin-binding Peptidasesmentioning

confidence: 99%

Peptidoglycan Hydrolases of Escherichia coli

Heijenoort

2011

Microbiol Mol Biol Rev

188

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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Bioconversion of anhydrosugars: Emerging concepts and strategies

Jarboe

2016

IUBMB Life

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As methods for the use of anhydrosugars in chemical and biofuel production continue to develop, our collective knowledge of anhydrosugar processing enzymes continues to improve, including their mechanistic details, structural dynamics and modes of substrate binding. Of particular interest, anhydrosugar kinases, such as levoglucosan kinase (LGK) and 1,6-anhydro-N-acetylmuramic acid kinase (AnmK), utilize an unusual mechanism whereby the sugar substrate is both cleaved and phosphorylated. The phosphorylated sugar can then be routed to other metabolic pathways, thereby allowing its further bioconversion. Advanced engineering efforts to improve the catalytic efficiency and stability of LGK have been steadily progressing. Other enzymes that cleave the glycosidic bond of disaccharide sugars containing an anhydrosugar component are also being identified and characterized. Accordingly, the potential future use of these enzymes in large-scale production strategies is becoming increasingly viable. Here, a mini-review of the observed characteristics of anhydrosugar processing enzymes is presented along with recent developments in the bioconversion of these sugars. V C 2016 IUBMB Life, 68(9): [700][701][702][703][704][705][706][707][708] 2016

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Scission of the Lactyl Ether Bond of N-Acetylmuramic Acid by Escherichia coli “Etherase”

Cited by 50 publications

References 31 publications

Two Modes of Autoregulation of themurRRepressor inEscherichia coli

Two Modes of Autoregulation of themurRRepressor inEscherichia coli

Peptidoglycan Hydrolases of Escherichia coli

Bioconversion of anhydrosugars: Emerging concepts and strategies

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