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  1. Article: N

    Hottmann, Isabel / Mayer, Valentina M T / Tomek, Markus B / Friedrich, Valentin / Calvert, Matthew B / Titz, Alexander / Schäffer, Christina / Mayer, Christoph

    Frontiers in microbiology

    2018  Volume 9, Page(s) 19

    Abstract: Tannerella ... ...

    Abstract Tannerella forsythia
    Language English
    Publishing date 2018-01-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2018.00019
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  2. Article ; Online: The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases.

    Müller, Maraike / Calvert, Matthew / Hottmann, Isabel / Kluj, Robert Maria / Teufel, Tim / Balbuchta, Katja / Engelbrecht, Alicia / Selim, Khaled A / Xu, Qingping / Borisova, Marina / Titz, Alexander / Mayer, Christoph

    The Journal of biological chemistry

    2021  Volume 296, Page(s) 100519

    Abstract: Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial ... bonds connecting N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). In contrast, little is ... known about exo-β-N-acetylmuramidases, which catalyze an exo-lytic cleavage of β-1,4-MurNAc entities ...

    Abstract Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that catalyze an endo-lytic cleavage of peptidoglycan; i.e., they hydrolyze the β-1,4-glycosidic bonds connecting N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). In contrast, little is known about exo-β-N-acetylmuramidases, which catalyze an exo-lytic cleavage of β-1,4-MurNAc entities from the non-reducing ends of peptidoglycan chains. Such an enzyme was identified earlier in the bacterium Bacillus subtilis, but the corresponding gene has remained unknown so far. We now report that ybbC of B. subtilis, renamed namZ, encodes the reported exo-β-N-acetylmuramidase. A ΔnamZ mutant accumulated specific cell wall fragments and showed growth defects under starvation conditions, indicating a role of NamZ in cell wall turnover and recycling. Recombinant NamZ protein specifically hydrolyzed the artificial substrate para-nitrophenyl β-MurNAc and the peptidoglycan-derived disaccharide MurNAc-β-1,4-GlcNAc. Together with the exo-β-N-acetylglucosaminidase NagZ and the exo-muramoyl-l-alanine amidase AmiE, NamZ degraded intact peptidoglycan by sequential hydrolysis from the non-reducing ends. A structure model of NamZ, built on the basis of two crystal structures of putative orthologs from Bacteroides fragilis, revealed a two-domain structure including a Rossmann-fold-like domain that constitutes a unique glycosidase fold. Thus, NamZ, a member of the DUF1343 protein family of unknown function, is now classified as the founding member of a new family of glycosidases (CAZy GH171; www.cazy.org/GH171.html). NamZ-like peptidoglycan hexosaminidases are mainly present in the phylum Bacteroidetes and less frequently found in individual genomes within Firmicutes (Bacilli, Clostridia), Actinobacteria, and γ-proteobacteria.
    MeSH term(s) Acetylglucosamine/metabolism ; Bacillus subtilis/enzymology ; Crystallography, X-Ray ; Glycoside Hydrolases/chemistry ; Glycoside Hydrolases/metabolism ; Hydrolysis ; Muramic Acids/metabolism ; Peptidoglycan/metabolism ; Protein Conformation
    Chemical Substances Muramic Acids ; Peptidoglycan ; N-acetylmuramic acid (246FXU111L) ; Glycoside Hydrolases (EC 3.2.1.-) ; endo-N-acetylmuramidase (EC 3.2.1.-) ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2021-03-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.100519
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  3. Article ; Online: An efficient synthesis of 1,6-anhydro- N -acetylmuramic acid from N -acetylglucosamine

    Calvert, Matthew B / Mayer, Christoph / Titz, Alexander

    2017  

    Publishing date 2017-12-11
    Publishing country de
    Document type Article ; Online
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  4. Article ; Online: An efficient synthesis of 1,6-anhydro- N -acetylmuramic acid from N -acetylglucosamine

    Calvert, Matthew B / Mayer, Christoph / Titz, Alexander

    2017  

    Publishing date 2017-12-11
    Publishing country de
    Document type Article ; Online
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  5. Article ; Online: An efficient synthesis of 1,6-anhydro-N-acetylmuramic acid from N-acetylglucosamine

    Matthew B. Calvert / Christoph Mayer / Alexander Titz

    Beilstein Journal of Organic Chemistry, Vol 13, Iss 1, Pp 2631-

    2017  Volume 2636

    Abstract: A novel synthesis of 1,6-anhydro-N-acetylmuramic acid is described, which proceeds in only five ... steps from the cheap starting material N-acetylglucosamine. This efficient synthesis should enable ...

    Abstract A novel synthesis of 1,6-anhydro-N-acetylmuramic acid is described, which proceeds in only five steps from the cheap starting material N-acetylglucosamine. This efficient synthesis should enable future studies into the importance of 1,6-anhydromuramic acid in bacterial cell wall recycling processes.
    Keywords N-acetylmuramic acid ; anhydrosugars ; antibiotic resistance ; bacterial cell wall recycling ; carbohydrate synthesis ; Science ; Q ; Organic chemistry ; QD241-441
    Language English
    Publishing date 2017-12-01T00:00:00Z
    Publisher Beilstein-Institut
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases.

    Müller, Maraike / Calvert, Matthew / Hottmann, Isabel / Kluj, Robert Maria / Teufel, Tim / Balbuchta, Katja / Engelbrecht, Alicia / Selim, Khaled A / Xu, Qingping / Borisova, Marina / Titz, Alexander / Mayer, Christoph

    296 ; 100519 ; The Journal of biological chemistry ; United States

    2021  

    Abstract: Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial ... bonds connecting N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). In contrast, little is ... known about exo-β-N-acetylmuramidases, which catalyze an exo-lytic cleavage of β-1,4-MurNAc entities ...

    Abstract Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that catalyze an endo-lytic cleavage of peptidoglycan; i.e., they hydrolyze the β-1,4-glycosidic bonds connecting N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). In contrast, little is known about exo-β-N-acetylmuramidases, which catalyze an exo-lytic cleavage of β-1,4-MurNAc entities from the non-reducing ends of peptidoglycan chains. Such an enzyme was identified earlier in the bacterium Bacillus subtilis, but the corresponding gene has remained unknown so far. We now report that ybbC of B. subtilis, renamed namZ, encodes the reported exo-β-N-acetylmuramidase. A ΔnamZ mutant accumulated specific cell wall fragments and showed growth defects under starvation conditions, indicating a role of NamZ in cell wall turnover and recycling. Recombinant NamZ protein specifically hydrolyzed the artificial substrate para-nitrophenyl β-MurNAc and the peptidoglycan-derived disaccharide MurNAc-β-1,4-GlcNAc. Together with the exo-β-N-acetylglucosaminidase NagZ and the exo-muramoyl-l-alanine amidase AmiE, NamZ degraded intact peptidoglycan by sequential hydrolysis from the non-reducing ends. A structure model of NamZ, built on the basis of two crystal structures of putative orthologs from Bacteroides fragilis, revealed a two-domain structure including a Rossmann-fold-like domain that constitutes a unique glycosidase fold. Thus, NamZ, a member of the DUF1343 protein family of unknown function, is now classified as the founding member of a new family of glycosidases (CAZy GH171; www.cazy.org/GH171.html). NamZ-like peptidoglycan hexosaminidases are mainly present in the phylum Bacteroidetes and less frequently found in individual genomes within Firmicutes (Bacilli, Clostridia), Actinobacteria, and γ-proteobacteria.
    Keywords N-acetylglucosaminidase ; N-acetylmuramidase ; N-acetylmuramoyl amidase ; Rossmann-fold ; cell wall recycling ; exo-lytic glycosidase ; lysozyme ; peptidoglycan hydrolase
    Subject code 572
    Language English
    Publishing date 2021-03-05
    Publisher Elsevier
    Publishing country de
    Document type Article ; Online
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  7. Article ; Online: N-Acetylmuramic Acid (MurNAc) Auxotrophy of the Oral PathogenTannerella forsythia

    Hottmann, Isabel / Mayer, Valentina M T / Tomek, Markus B / Friedrich, Valentin / Calvert, Matthew B / Titz, Alexander / Schäffer, Christina / Mayer, Christoph

    Characterization of a MurNAc Kinase and Analysis of Its Role in Cell Wall Metabolism.

    2018  

    Abstract: Tannerella forsythia is an anaerobic, Gram-negative oral pathogen that thrives in multispecies gingival biofilms associated with periodontitis. The bacterium is auxotrophic for the commonly essential bacterial cell wall sugarN-acetylmuramic acid (MurNAc) ...

    Abstract Tannerella forsythia is an anaerobic, Gram-negative oral pathogen that thrives in multispecies gingival biofilms associated with periodontitis. The bacterium is auxotrophic for the commonly essential bacterial cell wall sugarN-acetylmuramic acid (MurNAc) and, thus, strictly depends on an exogenous supply of MurNAc for growth and maintenance of cell morphology. A MurNAc transporter (Tf_MurT; Tanf_08375) and an ortholog of theEscherichia colietherase MurQ (Tf_MurQ; Tanf_08385) converting MurNAc-6-phosphate to GlcNAc-6-phosphate were recently described forT. forsythia.In between the respective genes on theT. forsythiagenome, a putative kinase gene is located. In this study, the putative kinase (Tf_MurK; Tanf_08380) was produced as a recombinant protein and biochemically characterized. Kinetic studies revealed Tf_MurK to be a 6-kinase with stringent substrate specificity for MurNAc exhibiting a 6 × 104-fold higher catalytic efficiency (kcat/Km) for MurNAc than forN-acetylglucosamine (GlcNAc) withkcatvalues of 10.5 s-1and 0.1 s-1andKmvalues of 200 μM and 116 mM, respectively. The enzyme kinetic data suggest that Tf_MurK is subject to substrate inhibition (Ki[S]= 4.2 mM). To assess the role of Tf_MurK in the cell wall metabolism ofT. forsythia, a kinase deletion mutant (ΔTf_murK::erm) was constructed. This mutant accumulated MurNAc intracellularly in the exponential phase, indicating the capability to take up MurNAc, but inability to catabolize MurNAc. In the stationary phase, the MurNAc level was reduced in the mutant, while the level of the peptidoglycan precursor UDP-MurNAc-pentapeptide was highly elevated. Further, according to scanning electron microscopy evidence, theΔTf_murK::ermmutant was more tolerant toward low MurNAc concentration in the medium (below 0.5 μg/ml) before transition from healthy, rod-shaped to fusiform cells occurred, while the parent strain required > 1 μg/ml MurNAc for optimal growth. These data reveal thatT. forsythiareadily catabolizes exogenous MurNAc but simultaneously channels a proportion of the sugar into peptidoglycan biosynthesis. Deletion ofTf_murKblocks MurNAc catabolism and allows the direction of MurNAc solely to peptidoglycan biosynthesis, resulting in a growth advantage in MurNAc-depleted medium. This work increases our understanding of theT. forsythiacell wall metabolism and may pave new routes for lead finding in the treatment of periodontitis.
    Subject code 580
    Language English
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: N-Acetylmuramic Acid (MurNAc) Auxotrophy of the Oral PathogenTannerella forsythia

    Hottmann, Isabel / Mayer, Valentina M T / Tomek, Markus B / Friedrich, Valentin / Calvert, Matthew B / Titz, Alexander / Schäffer, Christina / Mayer, Christoph

    Characterization of a MurNAc Kinase and Analysis of Its Role in Cell Wall Metabolism.

    2018  

    Abstract: Tannerella forsythia is an anaerobic, Gram-negative oral pathogen that thrives in multispecies gingival biofilms associated with periodontitis. The bacterium is auxotrophic for the commonly essential bacterial cell wall sugarN-acetylmuramic acid (MurNAc) ...

    Abstract Tannerella forsythia is an anaerobic, Gram-negative oral pathogen that thrives in multispecies gingival biofilms associated with periodontitis. The bacterium is auxotrophic for the commonly essential bacterial cell wall sugarN-acetylmuramic acid (MurNAc) and, thus, strictly depends on an exogenous supply of MurNAc for growth and maintenance of cell morphology. A MurNAc transporter (Tf_MurT; Tanf_08375) and an ortholog of theEscherichia colietherase MurQ (Tf_MurQ; Tanf_08385) converting MurNAc-6-phosphate to GlcNAc-6-phosphate were recently described forT. forsythia.In between the respective genes on theT. forsythiagenome, a putative kinase gene is located. In this study, the putative kinase (Tf_MurK; Tanf_08380) was produced as a recombinant protein and biochemically characterized. Kinetic studies revealed Tf_MurK to be a 6-kinase with stringent substrate specificity for MurNAc exhibiting a 6 × 104-fold higher catalytic efficiency (kcat/Km) for MurNAc than forN-acetylglucosamine (GlcNAc) withkcatvalues of 10.5 s-1and 0.1 s-1andKmvalues of 200 μM and 116 mM, respectively. The enzyme kinetic data suggest that Tf_MurK is subject to substrate inhibition (Ki[S]= 4.2 mM). To assess the role of Tf_MurK in the cell wall metabolism ofT. forsythia, a kinase deletion mutant (ΔTf_murK::erm) was constructed. This mutant accumulated MurNAc intracellularly in the exponential phase, indicating the capability to take up MurNAc, but inability to catabolize MurNAc. In the stationary phase, the MurNAc level was reduced in the mutant, while the level of the peptidoglycan precursor UDP-MurNAc-pentapeptide was highly elevated. Further, according to scanning electron microscopy evidence, theΔTf_murK::ermmutant was more tolerant toward low MurNAc concentration in the medium (below 0.5 μg/ml) before transition from healthy, rod-shaped to fusiform cells occurred, while the parent strain required > 1 μg/ml MurNAc for optimal growth. These data reveal thatT. forsythiareadily catabolizes exogenous MurNAc but simultaneously channels a proportion of the sugar into peptidoglycan biosynthesis. Deletion ofTf_murKblocks MurNAc catabolism and allows the direction of MurNAc solely to peptidoglycan biosynthesis, resulting in a growth advantage in MurNAc-depleted medium. This work increases our understanding of theT. forsythiacell wall metabolism and may pave new routes for lead finding in the treatment of periodontitis.
    Subject code 580
    Language English
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article: Cytoprotective effects of N,N,N-trimethylsphingosine during ischemia- reperfusion injury are lost in the setting of obesity and diabetes.

    Gundewar, Susheel / Calvert, John W / Elrod, John W / Lefer, David J

    American journal of physiology. Heart and circulatory physiology

    2007  Volume 293, Issue 4, Page(s) H2462–71

    Abstract: N,N,N-trimethylsphingosine chloride (TMS), a stable N-methylated synthetic sphingolipid analog, has ...

    Abstract N,N,N-trimethylsphingosine chloride (TMS), a stable N-methylated synthetic sphingolipid analog, has been shown to modulate protein kinase C (PKC) activity and exert a number of important biological effects, including inhibition of tumor cell growth and metastasis, inhibition of leukocyte migration and respiratory burst, and inhibition of platelet aggregation. We hypothesized that TMS would be cytoprotective in clinically relevant in vivo murine models of myocardial and hepatic ischemia-reperfusion (I/R) injury. Wild-type, obese (ob/ob), and diabetic (db/db) mice were subjected to 30 min of left coronary artery occlusion followed by 24 h of reperfusion in the myocardial I/R model. In additional studies, mice were subjected to 45 min of hepatic artery occlusion followed by 5 h of reperfusion. TMS was administered intravenously at the onset of ischemia. Myocardial infarct size, cardiac function, and serum liver enzymes were measured to assess the extent of tissue injury. TMS attenuated myocardial infarct size by 66% in the wild type and by 36% in the ob/ob mice. Furthermore, TMS reduced serum alanine transaminase levels by 43% in wild-type mice. These benefits did not extend to the ob/ob mice following hepatic I/R or to the db/db mice following both myocardial and hepatic I/R. A likely mechanism is the failure of TMS to inhibit PKC-delta translocation in the diseased heart. These data suggest that although TMS is cytoprotective following I/R in normal animals, the cytoprotective actions of TMS are largely attenuated in obese and diabetic animals.
    MeSH term(s) Animals ; Blood Glucose/metabolism ; Body Weight ; Cytoprotection ; Diabetes Mellitus, Type 2/complications ; Diabetes Mellitus, Type 2/genetics ; Diabetes Mellitus, Type 2/metabolism ; Diabetes Mellitus, Type 2/physiopathology ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Liver/blood supply ; Liver/drug effects ; Liver/pathology ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Mitochondria, Heart/drug effects ; Mitochondria, Heart/enzymology ; Myocardial Infarction/etiology ; Myocardial Infarction/prevention & control ; Myocardial Reperfusion Injury/complications ; Myocardial Reperfusion Injury/metabolism ; Myocardial Reperfusion Injury/pathology ; Myocardial Reperfusion Injury/physiopathology ; Myocardial Reperfusion Injury/prevention & control ; Myocardium/enzymology ; Myocardium/pathology ; Obesity/complications ; Obesity/genetics ; Obesity/metabolism ; Obesity/physiopathology ; Protective Agents/pharmacology ; Protective Agents/therapeutic use ; Protein Kinase C-delta/antagonists & inhibitors ; Protein Kinase C-delta/metabolism ; Protein Kinase Inhibitors/pharmacology ; Protein Kinase Inhibitors/therapeutic use ; Protein Transport ; Reperfusion Injury/complications ; Reperfusion Injury/metabolism ; Reperfusion Injury/pathology ; Reperfusion Injury/physiopathology ; Reperfusion Injury/prevention & control ; Sphingosine/analogs & derivatives ; Sphingosine/pharmacology ; Sphingosine/therapeutic use ; Time Factors ; Ventricular Function, Left/drug effects
    Chemical Substances Blood Glucose ; Protective Agents ; Protein Kinase Inhibitors ; N,N,N-trimethylsphingosine (138686-73-4) ; Protein Kinase C-delta (EC 2.7.11.13) ; Sphingosine (NGZ37HRE42)
    Language English
    Publishing date 2007-07-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 603838-4
    ISSN 1522-1539 ; 0363-6135
    ISSN (online) 1522-1539
    ISSN 0363-6135
    DOI 10.1152/ajpheart.00392.2007
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  10. Article ; Online: Mechanistic investigation of N,N-diethyl-4-(phenyl-piperidin-4-ylidenemethyl)-benzamide-induced insulin depletion in the rat and RINm5F cells.

    Otieno, Monicah A / Bavuso, Nicole / Milano, Joseph / Foster-Brown, Linda / Bui, Khanh-Hui / Li, Yan / Hudzik, Thomas / Wescott, Debra / Louden, Calvert / Dyroff, Martin / Pognan, François

    Toxicological sciences : an official journal of the Society of Toxicology

    2008  Volume 105, Issue 1, Page(s) 221–229

    Abstract: These studies describe the effect of N,N-diethyl-4-(phenyl-piperidin-4-ylidenemethyl)-benzamide (AR ...

    Abstract These studies describe the effect of N,N-diethyl-4-(phenyl-piperidin-4-ylidenemethyl)-benzamide (AR-M100390), a delta-opioid agonist, on the pancreas and its mechanisms for pancreatic toxicity. Rats were treated with 5, 100, and 600 micromol/kg of AR-M100390 for 3 and/or 7 days; another group of rats treated with 600 micromol/kg of compound were allowed to recover for 14 days. AR-M100390 (600 micromol/kg) caused vacuolation in the beta-cell of the rat pancreas that was associated with depletion of insulin and hyperglycemia after 7 days of dosing. The loss of insulin by AR-M100390 was due to specific inhibition of rat insulin2 mRNA transcription in vivo. Insulin depletion and hyperglycemia were reversible. The effects of AR-M100390 in rats were reproduced in the rat pancreatic beta-cell line RINm5F, where it inhibited intracellular insulin content and secretion without affecting cell survival. Loss of insulin in vitro was also a result of specific inhibition of insulin2 mRNA transcription and was reversible. Pretreatment of cells with the delta-opioid antagonist naltrindole or pertussis toxin did not reverse loss of insulin in AR-M100390-treated cells suggesting that the effects were not mediated by the delta-opioid receptor. AR-M100390 inhibited KCl-mediated calcium mobilization in RINm5F cells, suggesting that L-type calcium channels found in these cells and in pancreatic beta-cells may partially play a role in the inhibition of insulin secretion by this compound. In summary, the in vitro and in vivo studies suggest that inhibition of insulin by AR-M100390 is due to a combination of inhibition of insulin synthesis and/or release.
    MeSH term(s) Animals ; Benzamides/toxicity ; Blood Glucose/analysis ; Calcium/metabolism ; Calcium Channels, L-Type/physiology ; Cells, Cultured ; Cyclizine/toxicity ; Dose-Response Relationship, Drug ; Insulin/genetics ; Insulin/metabolism ; Pancreas/drug effects ; Pancreas/metabolism ; Piperidines/toxicity ; RNA, Messenger/analysis ; Rats ; Rats, Wistar ; Receptors, Opioid, delta/agonists
    Chemical Substances Benzamides ; Blood Glucose ; Calcium Channels, L-Type ; Insulin ; N,N-diethyl-4-(phenylpiperidin-4-ylidenemethyl)benzamide ; Piperidines ; RNA, Messenger ; Receptors, Opioid, delta ; Cyclizine (QRW9FCR9P2) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2008-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1420885-4
    ISSN 1096-0929 ; 1096-6080
    ISSN (online) 1096-0929
    ISSN 1096-6080
    DOI 10.1093/toxsci/kfn108
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