Peptidoglycan biosynthesis in Micrococcus luteus (sodonensis): transglycosidase and phosphodiesterase activities in membrane preparations

Jensen, Susan E.; Campbell, James N.

doi:10.1128/jb.127.1.309-318.1976

Cited by 8 publications

(11 citation statements)

References 25 publications

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“…As well as residual substrate (peak II, retardation factor [R1] = 0.3) present in both systems, exponential phase-membrane chromatograms showed a new peak of radioactivity (peak III), the amidase product. This material was demonstrated by paper chromatography not to be free alanine or MurNAc-['4C]pentapeptide and therefore was not the result of either transpeptidase, DD-carboxypeptidase, or phosphodiesterase activity (10). To investigate the possibility that the new material was the result of peptidoglycan breakdown, a type 1 amidase assay was performed.…”

Section: Resultsmentioning

confidence: 99%

“…Enzyme assays. Transglycosidase assays were performed as described elsewhere (10). N-acetylmuramyl-L-alanine amidase activity was assayed by two methods.…”

Section: Downloaded Frommentioning

confidence: 99%

“…MATERIALS AND METHODS UDP-MurNAc-P4C]pentapeptide. Uridine diphosphate -Nacetylmuramyl -Lalanyl -Disoglutamyl-L-lysyl-D-alanyl-D-alanine (UDP-MurNAc-[14C]pentapeptide) was prepared as previously described (10). Radioactivity was distributed among the three alanine residues of the peptide, and the purified material had a specific activity of 694 dpm/nmol.…”

mentioning

confidence: 99%

“…In vitro-synthesized peptidoglycan. In vitro-synthesized peptidoglycan was prepared and partially purified as previously described (10).…”

mentioning

confidence: 99%

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Amidase activity involved in peptidoglycan biosynthesis in membranes of Micrococcus luteus (sodonensis)

Jensen¹,

Campbell²

1976

J Bacteriol

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Membrane suspensions prepared from Micrococcus luteus (sodonensis) in both the exponential and stationary phases of growth contained a transglycosidase activity capable of synthesizing linear peptidoglycan. Exponential-phase membranes also contained an N-acetylmuramyl-L-alanine amidase activity which degraded the peptidoglycan as it was formed. The product of this amidase was purified and found to be free pentapeptide. The amidase was specific for peptidoglycan and could not attack lower-molecular-weight substrates even though the susceptible bond was present. Crude cell wall preparations isolated from exponential-phase cells also contained high levels of amidase. This cell wall-bound amidase would preferentially degrade in vitro-synthesized peptidoglycan over its own cell wall. Amidase activity could be solubilized from both cell walls and membranes by Triton X-100 treatment, butanol extraction, or LiCl extraction. Both membrane- and cell wall-derived amidases, solubilized by LiCl extraction, appeared to be of high molecular weight (greater than 150,000). Once solubilized, these wall- and membrane-derived amidases could attack the cross-bridged peptidoglycan of purified native cell walls, whereas bound amidases could not.

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Section: Resultsmentioning

confidence: 99%

“…Enzyme assays. Transglycosidase assays were performed as described elsewhere (10). N-acetylmuramyl-L-alanine amidase activity was assayed by two methods.…”

Section: Downloaded Frommentioning

confidence: 99%

mentioning

confidence: 99%

“…In vitro-synthesized peptidoglycan. In vitro-synthesized peptidoglycan was prepared and partially purified as previously described (10).…”

mentioning

confidence: 99%

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Amidase activity involved in peptidoglycan biosynthesis in membranes of Micrococcus luteus (sodonensis)

Jensen¹,

Campbell²

1976

J Bacteriol

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“…was chosen due to its highly frequent presence in foodborne outbreaks, being lethal in many cases. Micrococcus luteus is not a severe pathogenic bacterium, but for many years it has been used as a model system for bacterial cell wall study due to low peptidoglycan cross-linking (about 25%) [30,31]. M. luteus sensitivity to cell wall disruption was the reason to choose this microorganism as Gram-positive model.…”

Section: Minimum Inhibitory Concentrationmentioning

confidence: 99%

Rheological and Antimicrobial Properties of Chitosan and Quinoa Protein Filmogenic Suspensions with Thyme and Rosemary Essential Oils

Escamilla‐García

Ríos-Romo

Melgarejo-Mancilla

et al. 2020

Foods

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Food packaging faces the negative impact of synthetic materials on the environment, and edible coatings offer one alternative from filmogenic suspensions (FS). In this work, an active edible FS based on chitosan (C) and quinoa protein (QP) cross-linked with transglutaminase was produced. Thyme (T) and rosemary (R) essential oils (EOs) were incorporated as antimicrobial agents. Particle size, Z potential, and rheological parameters were evaluated. The antimicrobial activity against Micrococcus luteus (NCIB 8166) and Salmonella sp. (Lignieres 1900) was monitored using atomic force microscopy and image analysis. Results indicate that EOs incorporation into C:QP suspensions did not affect the Z potential, ranging from −46.69 ± 3.19 mV to −46.21 ± 3.83 mV. However, the polydispersity index increased from 0.51 ± 0.07 to 0.80 ± 0.04 in suspensions with EO. The minimum inhibitory concentration of active suspensions against Salmonella sp. was 0.5% (v/v) for thyme and 1% (v/v) for rosemary. Entropy and fractal dimension of the images were used to confirm the antimicrobial effect of EOs, which modified the surface roughness.

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Effect of growth temperature on the externalization and localization of α‐amylase in Bacillus stearothermophilus

Bezbaruah¹,

Pillai²,

Gogoi³

et al. 1987

J. Basic Microbiol.

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The synthesis and localization of a-amylase were studied in Bacillus stearothermophilus AN002 at 40,45,50 and 55 "C and also during early exponential, late exponential and stationary phases of growth. The extracellular a-amylase synthesis was highest at 50 "C and at stationary growth phase. Accumulation of intracellular a-amylase was observed in cells grown at 40 "C and was distributed in all the cell fractions. At 50 and 55 "C the cell did not have a-amylase in the protoplasm or protoplasmic membrane. The synthesis and externalization of extracellular enzyme are two processes and the externalization is controlled by growth temperature and cell age. Since little is known about the external factors and cell age that regulate the synthesis and localization of the extracellular enzymes, we have examined the production and cellular localization of a-amylase under different growth temperature and at various stages of growth. We have also attempted to correlate the synthesis and externalization of exoenzyme as a function of growth temperature and cell age.

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Peptidoglycan biosynthesis in Micrococcus luteus (sodonensis): transglycosidase and phosphodiesterase activities in membrane preparations

Cited by 8 publications

References 25 publications

Amidase activity involved in peptidoglycan biosynthesis in membranes of Micrococcus luteus (sodonensis)

Amidase activity involved in peptidoglycan biosynthesis in membranes of Micrococcus luteus (sodonensis)

Rheological and Antimicrobial Properties of Chitosan and Quinoa Protein Filmogenic Suspensions with Thyme and Rosemary Essential Oils

Effect of growth temperature on the externalization and localization of α‐amylase in Bacillus stearothermophilus

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