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Draft Genome Sequence of Bacillus clausii AKU0647, a Strain That Produces Endo-β-N-Acetylglucosaminidase A.

Genome announcements

Higuchi Y, Mori K, Suyama A, Huang Y, Tashiro K, Kuhara S, Takegawa K.
PMID: 27151792
Genome Announc. 2016 May 05;4(3). doi: 10.1128/genomeA.00310-16.

To comprehensively identify glycosyl hydrolase genes in the genome of Bacillus clausii strain AKU0647, which produces endo-β-N-acetylglucosaminidase A (Endo-A), we conducted whole-genome shotgun sequencing. We identified several other putative glycosyl hydrolase genes apart from the Endo-A gene, and report...

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Higuchi Y, Mori K, Suyama A, et al. Draft Genome Sequence of Bacillus clausii AKU0647, a Strain That Produces Endo-β-N-Acetylglucosaminidase A. Genome Announc. 2016;4(3)doi: 10.1128/genomeA.00310-16.
Higuchi, Y., Mori, K., Suyama, A., Huang, Y., Tashiro, K., Kuhara, S., & Takegawa, K. (2016). Draft Genome Sequence of Bacillus clausii AKU0647, a Strain That Produces Endo-β-N-Acetylglucosaminidase A. Genome announcements, 4(3), . https://doi.org/10.1128/genomeA.00310-16
Higuchi, Yujiro, et al. "Draft Genome Sequence of Bacillus clausii AKU0647, a Strain That Produces Endo-β-N-Acetylglucosaminidase A." Genome announcements vol. 4,3 (2016). doi: https://doi.org/10.1128/genomeA.00310-16
Higuchi Y, Mori K, Suyama A, Huang Y, Tashiro K, Kuhara S, Takegawa K. Draft Genome Sequence of Bacillus clausii AKU0647, a Strain That Produces Endo-β-N-Acetylglucosaminidase A. Genome Announc. 2016 May 05;4(3). doi: 10.1128/genomeA.00310-16. PMID: 27151792; PMCID: PMC4859174.
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Polypeptide pattern and enzymic character of vacuoles isolated from barley mesophyll protoplasts.

Planta

Kaiser G, Martinoia E, Schmitt JM, Hincha DK, Heber U.
PMID: 24232646
Planta. 1986 Nov;169(3):345-55. doi: 10.1007/BF00392130.

Intact chloroplasts and vacuoles were isolated from mesophyll protoplasts of barley. The chloroplasts occupied about 15% of the cellular volume and contained 75% of the protein, whereas the vacuoles occupied about 80% of the volume and contained less than...

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Kaiser G, Martinoia E, Schmitt JM, et al. Polypeptide pattern and enzymic character of vacuoles isolated from barley mesophyll protoplasts. Planta. 1986;169(3):345-55doi: 10.1007/BF00392130.
Kaiser, G., Martinoia, E., Schmitt, J. M., Hincha, D. K., & Heber, U. (1986). Polypeptide pattern and enzymic character of vacuoles isolated from barley mesophyll protoplasts. Planta, 169(3), 345-55. https://doi.org/10.1007/BF00392130
Kaiser, G, et al. "Polypeptide pattern and enzymic character of vacuoles isolated from barley mesophyll protoplasts." Planta vol. 169,3 (1986): 345-55. doi: https://doi.org/10.1007/BF00392130
Kaiser G, Martinoia E, Schmitt JM, Hincha DK, Heber U. Polypeptide pattern and enzymic character of vacuoles isolated from barley mesophyll protoplasts. Planta. 1986 Nov;169(3):345-55. doi: 10.1007/BF00392130. PMID: 24232646.
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Ref cell hydrolases: Glycosidase activities in human erythrocyte plasma membranes.

The Journal of membrane biology

Bosmann HB.
PMID: 24174233
J Membr Biol. 1971 Dec;4(1):113-23. doi: 10.1007/BF02431965.

Human erythrocyte plasma membranes were found to contain the following glycosidases: α- and β-glucosidase, α- and β-galactosidase, α- and β-fucosidase, β-N-acetylglucosaminidase, β-N-acetylgalactosaminidase, β-xylosidase and α-mannosidase. All the enzymes except β-fucosidase had activity interpreted to be on the external surface...

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Bosmann HB. Ref cell hydrolases: Glycosidase activities in human erythrocyte plasma membranes. J Membr Biol. 1971;4(1):113-23doi: 10.1007/BF02431965.
Bosmann, H. B. (1971). Ref cell hydrolases: Glycosidase activities in human erythrocyte plasma membranes. The Journal of membrane biology, 4(1), 113-23. https://doi.org/10.1007/BF02431965
Bosmann, H B. "Ref cell hydrolases: Glycosidase activities in human erythrocyte plasma membranes." The Journal of membrane biology vol. 4,1 (1971): 113-23. doi: https://doi.org/10.1007/BF02431965
Bosmann HB. Ref cell hydrolases: Glycosidase activities in human erythrocyte plasma membranes. J Membr Biol. 1971 Dec;4(1):113-23. doi: 10.1007/BF02431965. PMID: 24174233.
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Evaluation of Extracellular, High-affinity beta-N-acetylglucosaminidase Measurements from Freshwater Lakes: An Enzyme Assay to Estimate Protistan Grazing on Bacteria and Picocyanobacteria.

Microbial ecology

Vrba J, Simek K, Pernthaler J, Psenner R.
PMID: 8661544
Microb Ecol. 1996 Jul;32(1):81-99.

Protistan community grazing rates upon both bacterioplankton and autotrophic picoplankton were estimated using fluorescently-labeled prey and by measurement of extracellular hydrolysis of 4-methylumbelliferyl (MUF) beta-N-acetylglucosaminide in a eutrophic reservoir and an oligo-mesotrophic lake during phytoplankton blooms. In addition, enzyme...

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Vrba J, Simek K, Pernthaler J, et al. Evaluation of Extracellular, High-affinity beta-N-acetylglucosaminidase Measurements from Freshwater Lakes: An Enzyme Assay to Estimate Protistan Grazing on Bacteria and Picocyanobacteria. Microb Ecol. 1996;32(1):81-99
Vrba, J., Simek, K., Pernthaler, J., & Psenner, R. (1996). Evaluation of Extracellular, High-affinity beta-N-acetylglucosaminidase Measurements from Freshwater Lakes: An Enzyme Assay to Estimate Protistan Grazing on Bacteria and Picocyanobacteria. Microbial ecology, 32(1), 81-99.
Vrba, et al. "Evaluation of Extracellular, High-affinity beta-N-acetylglucosaminidase Measurements from Freshwater Lakes: An Enzyme Assay to Estimate Protistan Grazing on Bacteria and Picocyanobacteria." Microbial ecology vol. 32,1 (1996): 81-99.
Vrba J, Simek K, Pernthaler J, Psenner R. Evaluation of Extracellular, High-affinity beta-N-acetylglucosaminidase Measurements from Freshwater Lakes: An Enzyme Assay to Estimate Protistan Grazing on Bacteria and Picocyanobacteria. Microb Ecol. 1996 Jul;32(1):81-99. PMID: 8661544.
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Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine.

Plant physiology

Hori H, Kaushal GP, Elbein AD.
PMID: 16664119
Plant Physiol. 1985 Mar;77(3):687-94. doi: 10.1104/pp.77.3.687.

Cultures of soybean cells incorporate [5,6-(3)H]-l-fucose into various cellular components including lipids and proteins. The membrane glyco-proteins were digested with pronase to produce glycopeptides, and the glycopeptides were isolated on columns of Biogel P-4. The major fucoselabeled glycopeptide sized...

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Hori H, Kaushal GP, Elbein AD. Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant Physiol. 1985;77(3):687-94doi: 10.1104/pp.77.3.687.
Hori, H., Kaushal, G. P., & Elbein, A. D. (1985). Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant physiology, 77(3), 687-94. https://doi.org/10.1104/pp.77.3.687
Hori, H, et al. "Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine." Plant physiology vol. 77,3 (1985): 687-94. doi: https://doi.org/10.1104/pp.77.3.687
Hori H, Kaushal GP, Elbein AD. Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant Physiol. 1985 Mar;77(3):687-94. doi: 10.1104/pp.77.3.687. PMID: 16664119; PMCID: PMC1064585.
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Cloning, nucleotide sequence and expression of the beta-N-acetylglucosaminidase gene from Aeromonas sp. no. 10S-24.

Journal of bioscience and bioengineering

Ueda M, Fujita Y, Kawaguchi T, Arai M.
PMID: 16232720
J Biosci Bioeng. 2000;89(2):164-9. doi: 10.1016/s1389-1723(00)88731-9.

The beta-GlcNAcase gene of Aeromonas sp. no. 10S-24 was cloned and sequenced. The gene consisted of 2505 bp encoding 835 amino acid residues. The amino acid sequence of the gene shares sequence homology with beta-GlcNAcases of Vibrio vulnificus (37.4%),...

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Ueda M, Fujita Y, Kawaguchi T, et al. Cloning, nucleotide sequence and expression of the beta-N-acetylglucosaminidase gene from Aeromonas sp. no. 10S-24. J Biosci Bioeng. 2000;89(2):164-9doi: 10.1016/s1389-1723(00)88731-9.
Ueda, M., Fujita, Y., Kawaguchi, T., & Arai, M. (2000). Cloning, nucleotide sequence and expression of the beta-N-acetylglucosaminidase gene from Aeromonas sp. no. 10S-24. Journal of bioscience and bioengineering, 89(2), 164-9. https://doi.org/10.1016/s1389-1723(00)88731-9
Ueda, M, et al. "Cloning, nucleotide sequence and expression of the beta-N-acetylglucosaminidase gene from Aeromonas sp. no. 10S-24." Journal of bioscience and bioengineering vol. 89,2 (2000): 164-9. doi: https://doi.org/10.1016/s1389-1723(00)88731-9
Ueda M, Fujita Y, Kawaguchi T, Arai M. Cloning, nucleotide sequence and expression of the beta-N-acetylglucosaminidase gene from Aeromonas sp. no. 10S-24. J Biosci Bioeng. 2000;89(2):164-9. doi: 10.1016/s1389-1723(00)88731-9. PMID: 16232720.
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Chemo-enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase.

Journal of bioscience and bioengineering

Yamamoto K.
PMID: 16233137
J Biosci Bioeng. 2001;92(6):493-501. doi: 10.1263/jbb.92.493.

The chemo-enzymatic synthesis of a glycopeptide, which involves the chemical synthesis of N-acetylglucosaminyl peptide and the enzymatic transfer of oligosaccharide, is described. The first step of the chemo-enzymatic method is the chemical synthesis of N-acetylglucosaminyl peptide with an N-acetylglucosamine...

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Yamamoto K. Chemo-enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase. J Biosci Bioeng. 2001;92(6):493-501doi: 10.1263/jbb.92.493.
Yamamoto, K. (2001). Chemo-enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase. Journal of bioscience and bioengineering, 92(6), 493-501. https://doi.org/10.1263/jbb.92.493
Yamamoto, K. "Chemo-enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase." Journal of bioscience and bioengineering vol. 92,6 (2001): 493-501. doi: https://doi.org/10.1263/jbb.92.493
Yamamoto K. Chemo-enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase. J Biosci Bioeng. 2001;92(6):493-501. doi: 10.1263/jbb.92.493. PMID: 16233137.
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Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor.

Microbial cell factories

Shao X, Jiang M, Yu Z, Cai H, Li L.
PMID: 19754974
Microb Cell Fact. 2009 Sep 16;8:48. doi: 10.1186/1475-2859-8-48.

BACKGROUND: Previous studies have revealed that the lysin motif (LysM) domains of bacterial cell wall-degrading enzymes are able to bind to peptidoglycan moieties of the cell wall. This suggests an approach for a cell surface display system in Gram-positive...

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Shao X, Jiang M, Yu Z, et al. Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor. Microb Cell Fact. 2009;8:48doi: 10.1186/1475-2859-8-48.
Shao, X., Jiang, M., Yu, Z., Cai, H., & Li, L. (2009). Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor. Microbial cell factories, 848. https://doi.org/10.1186/1475-2859-8-48
Shao, Xiaohu, et al. "Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor." Microbial cell factories vol. 8 (2009): 48. doi: https://doi.org/10.1186/1475-2859-8-48
Shao X, Jiang M, Yu Z, Cai H, Li L. Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor. Microb Cell Fact. 2009 Sep 16;8:48. doi: 10.1186/1475-2859-8-48. PMID: 19754974; PMCID: PMC2754439.
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Production of Extracellular Proteins by the Biocontrol Fungus Gliocladium virens.

Applied and environmental microbiology

van Tilburg AU, Thomas MD.
PMID: 16348848
Appl Environ Microbiol. 1993 Jan;59(1):236-42. doi: 10.1128/aem.59.1.236-242.1993.

Gliocladium virens is a common saprophytic fungus that is mycoparasitic on a large number of fungi. Responses of G. virens toward its environment were examined by monitoring the presence of extracellular proteins in culture fluid during time course experiments....

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van Tilburg AU, Thomas MD. Production of Extracellular Proteins by the Biocontrol Fungus Gliocladium virens. Appl Environ Microbiol. 1993;59(1):236-42doi: 10.1128/aem.59.1.236-242.1993.
van Tilburg, A. U., & Thomas, M. D. (1993). Production of Extracellular Proteins by the Biocontrol Fungus Gliocladium virens. Applied and environmental microbiology, 59(1), 236-42. https://doi.org/10.1128/aem.59.1.236-242.1993
van Tilburg, A U, and Thomas, M D. "Production of Extracellular Proteins by the Biocontrol Fungus Gliocladium virens." Applied and environmental microbiology vol. 59,1 (1993): 236-42. doi: https://doi.org/10.1128/aem.59.1.236-242.1993
van Tilburg AU, Thomas MD. Production of Extracellular Proteins by the Biocontrol Fungus Gliocladium virens. Appl Environ Microbiol. 1993 Jan;59(1):236-42. doi: 10.1128/aem.59.1.236-242.1993. PMID: 16348848; PMCID: PMC202084.
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Relating microbial community structure to functioning in forest soil organic carbon transformation and turnover.

Ecology and evolution

You Y, Wang J, Huang X, Tang Z, Liu S, Sun OJ.
PMID: 25035803
Ecol Evol. 2014 Mar;4(5):633-47. doi: 10.1002/ece3.969. Epub 2014 Feb 12.

Forest soils store vast amounts of terrestrial carbon, but we are still limited in mechanistic understanding on how soil organic carbon (SOC) stabilization or turnover is controlled by biotic and abiotic factors in forest ecosystems. We used phospholipid fatty...

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You Y, Wang J, Huang X, et al. Relating microbial community structure to functioning in forest soil organic carbon transformation and turnover. Ecol Evol. 2014;4(5):633-47doi: 10.1002/ece3.969.
You, Y., Wang, J., Huang, X., Tang, Z., Liu, S., & Sun, O. J. (2014). Relating microbial community structure to functioning in forest soil organic carbon transformation and turnover. Ecology and evolution, 4(5), 633-47. https://doi.org/10.1002/ece3.969
You, Yeming, et al. "Relating microbial community structure to functioning in forest soil organic carbon transformation and turnover." Ecology and evolution vol. 4,5 (2014): 633-47. doi: https://doi.org/10.1002/ece3.969
You Y, Wang J, Huang X, Tang Z, Liu S, Sun OJ. Relating microbial community structure to functioning in forest soil organic carbon transformation and turnover. Ecol Evol. 2014 Mar;4(5):633-47. doi: 10.1002/ece3.969. Epub 2014 Feb 12. PMID: 25035803; PMCID: PMC4098142.
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A facile synthesis of a complex type N-glycan thiazoline as an effective inhibitor against the antibody-deactivating endo-β-N-acetylglucosaminidases.

Journal of carbohydrate chemistry

Li C, Zhu S, Tong X, Ou C, Wang LX.
PMID: 30930529
J Carbohydr Chem. 2017;36(8):336-346. doi: 10.1080/07328303.2017.1403616. Epub 2017 Dec 07.

Endo-β-N-acetylglucosaminidases are a class of endoglycosidases that deglycosylate N-glycans from glycoproteins. We describe here a facile synthesis of a complex type N-glycan thiazoline as a new mechanism-based inhibitor for this class of enzymes. The synthesis started with the readily...

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Li C, Zhu S, Tong X, et al. A facile synthesis of a complex type N-glycan thiazoline as an effective inhibitor against the antibody-deactivating endo-β-N-acetylglucosaminidases. J Carbohydr Chem. 2017;36(8):336-346doi: 10.1080/07328303.2017.1403616.
Li, C., Zhu, S., Tong, X., Ou, C., & Wang, L. X. (2017). A facile synthesis of a complex type N-glycan thiazoline as an effective inhibitor against the antibody-deactivating endo-β-N-acetylglucosaminidases. Journal of carbohydrate chemistry, 36(8), 336-346. https://doi.org/10.1080/07328303.2017.1403616
Li, Chao, et al. "A facile synthesis of a complex type N-glycan thiazoline as an effective inhibitor against the antibody-deactivating endo-β-N-acetylglucosaminidases." Journal of carbohydrate chemistry vol. 36,8 (2017): 336-346. doi: https://doi.org/10.1080/07328303.2017.1403616
Li C, Zhu S, Tong X, Ou C, Wang LX. A facile synthesis of a complex type N-glycan thiazoline as an effective inhibitor against the antibody-deactivating endo-β-N-acetylglucosaminidases. J Carbohydr Chem. 2017;36(8):336-346. doi: 10.1080/07328303.2017.1403616. Epub 2017 Dec 07. PMID: 30930529; PMCID: PMC6436815.
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Erratum: Molecular evolution and transcriptional profile of GH3 and GH20 β-N-acetylglucosaminidases in the entomopathogenic fungus.

Genetics and molecular biology

[No authors listed]
PMID: 30816907
Genet Mol Biol. 2019 Feb 28;42(1):151. doi: 10.1590/1678-4685-gmb-2017-0363er. Epub 2019 Feb 28.

No abstract available.

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Erratum: Molecular evolution and transcriptional profile of GH3 and GH20 β-N-acetylglucosaminidases in the entomopathogenic fungus. Genet Mol Biol. 2019;42(1):151doi: 10.1590/1678-4685-gmb-2017-0363er.
(2019). Erratum: Molecular evolution and transcriptional profile of GH3 and GH20 β-N-acetylglucosaminidases in the entomopathogenic fungus. Genetics and molecular biology, 42(1), 151. https://doi.org/10.1590/1678-4685-gmb-2017-0363er
"Erratum: Molecular evolution and transcriptional profile of GH3 and GH20 β-N-acetylglucosaminidases in the entomopathogenic fungus." Genetics and molecular biology vol. 42,1 (2019): 151. doi: https://doi.org/10.1590/1678-4685-gmb-2017-0363er
Erratum: Molecular evolution and transcriptional profile of GH3 and GH20 β-N-acetylglucosaminidases in the entomopathogenic fungus. Genet Mol Biol. 2019 Feb 28;42(1):151. doi: 10.1590/1678-4685-gmb-2017-0363er. Epub 2019 Feb 28. PMID: 30816907; PMCID: PMC6428120.
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Showing 1 to 12 of 136 entries