Activity Assay:
Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Mutagenesis:Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Molecular Cloning:Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Expressing:Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Purification:Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Nuclear Magnetic Resonance:Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Comparison:Article Title: Unveiling the Transgalactosylation Switch of a GH42 β‑Galactosidase from the Infant Isolate Bifidobacterium breve DSM20213
Article Snippet: .. The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c08164 Primers used in this study (Table S1); Superimposition of active-site amino acid residues of GH42 Bbre βgal-III onto GH42 Bi Bga42A from B. longum subsp. infantis ATCC 15697 and GH42 BbgII from B. bifidum S17 (Figure S1); Site-saturation mutagenesis of Arg121 in Bbre βgal-III from molecular cloning to protein expression and purification (Figure S2); Distribution of R121 variants in terms of relative enzyme and transgalactosylation activities to wild-type Bbre βgal-III (Figure S3); Representative HPAEC-PAD chromatograms for GOS analysis (Figure S4); Size distribution of GOS formed during the lactose conversion by Bbre βgal-III-R121C using HPSEC-UV (Figure S5); (A) 1 H NMR spectrum of the disaccharide fraction; (B) Comparison of 1 H NMR spectra of the trisaccharide fraction of Bbre βgal-III-R121C and Bbre βgal-III-wild type (Figure S6); 1 H NMR comparison of penta- (A) and tetrasaccharide (B) fractions (Figure S7); Occurrence of hydrogen bonds during the molecular dynamics simulations (Figure S8); Representation of the number of waters associated with the tunnels as a function of simulation time (Figure S9); Comparison of the water tunnels of two GH42 β-galactosidases from B. bifidum S17 and B. longum subsp. infantis ATCC 15697 with Bbre βgal-III (Figure S10); Amino acids lining the water tunnel A of GH42 β-galactosidases found in the UniProt database (Figure S11); and pH dependency of enzyme activity (Figure S12) ( PDF ) ..
Sequencing:
other:
Article Title: Insights into toxin-antitoxin systems in the genus Bifidobacterium
Article Snippet: All MazF toxins from B. longum subsp. infantis ATCC 15697 was highly toxic in E. coli in the absence of their cognate antitoxin genes, and their mRNA transcripts increased in the nutrient-depleted conditions of late stationary culture in the B. longum host ( ).
Article Title: Insights into toxin-antitoxin systems in the genus Bifidobacterium
Article Snippet: Interestingly, in B. longum subsp. infantis ATCC 15697, all the identified toxin components of the TA systems belong to different families—MazF, RelE, and VapC—while all the corresponding antitoxins are members of the RelB family ( ).
Residue:
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