m0392  (New England Biolabs)


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    New England Biolabs m0392
    M0392, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    m0392 - by Bioz Stars, 2022-05
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    • β agarase  (New England Biolabs)
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    New England Biolabs β agarase
    Multiple alignment of <t>β-agarase</t> amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).
    β Agarase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Multiple alignment of β-agarase amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).

    Journal: Brazilian Journal of Microbiology

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    doi: 10.1590/S1517-83822010000400006

    Figure Lengend Snippet: Multiple alignment of β-agarase amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).

    Article Snippet: Neoagarohexanitol (NA6) was purchased from Sigma (USA) and neoagarotetraose (NA4) and neoagarobiose (NA2) (NA4 + NA2) were prepared by digestion of neoagarohexanitol using commercial β-agarase (New England Biolab, USA).

    Techniques: Binding Assay, Sequencing

    Phylogenetic analysis of AgaA with known agarases based on amino acid sequence. Phylogenetic analysis was done by the Neighbor Joining method using MEGA3.1, based on sequence alignment using ClustalW (1.81). Numbers indicate the bootstrap confidence values of 1000 replicates. The accession numbers of the selected agarase sequences are as follows: AB178483, agarase ( Agarivorans sp. JAMB-A11); EF051475, QM38 agarase ( Agarivorans sp. QM38); EF100136, β-agarase ( Agarivorans sp. JA-1); AAA25696, β-agarase precursor ( Pseudoalteromonas atlantica ); AAP49346, AguB; AAP70390, AguH; AAP70365, AguK; AAP49316, AguD from uncultured bacterium; AAA91888, β-agarase I ( Pseudoalteromonas atlantica ); AAF03246, β-agarase ( Aeromonas sp.); AB124837, agarase ( Microbulbifer thermotolerans ); BAC99022, agarase ( Microbulbifer elongatus ); BAB79291, agarase, ( Pseudomonas sp. ND137; AAF21821, β-agarase B precursor ( Zobellia galactanivorans ); AAF21820, β-agarase A precursor ( Zobellia galactanivorans ); AAN39119, extracellular agarase precursor, ( Pseudoalteromonas sp. CY24); CAB61795, extracellular agarase precursor ( Streptomyces coelicolor A3); AAP70364, AguJ (uncultured bacterium); BAA04744, β-agarase ( Vibrio sp.); BAA03541, β-agarase ( Vibrio sp. JT0107); BAH16616, agarase ( Cellvibrio sp. OA-2007); AAT67062, β-agarase I ( Saccharophagus degradans ); AB160954, β-agarase ( Microbulbifer thermotolerans ).

    Journal: Brazilian Journal of Microbiology

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    doi: 10.1590/S1517-83822010000400006

    Figure Lengend Snippet: Phylogenetic analysis of AgaA with known agarases based on amino acid sequence. Phylogenetic analysis was done by the Neighbor Joining method using MEGA3.1, based on sequence alignment using ClustalW (1.81). Numbers indicate the bootstrap confidence values of 1000 replicates. The accession numbers of the selected agarase sequences are as follows: AB178483, agarase ( Agarivorans sp. JAMB-A11); EF051475, QM38 agarase ( Agarivorans sp. QM38); EF100136, β-agarase ( Agarivorans sp. JA-1); AAA25696, β-agarase precursor ( Pseudoalteromonas atlantica ); AAP49346, AguB; AAP70390, AguH; AAP70365, AguK; AAP49316, AguD from uncultured bacterium; AAA91888, β-agarase I ( Pseudoalteromonas atlantica ); AAF03246, β-agarase ( Aeromonas sp.); AB124837, agarase ( Microbulbifer thermotolerans ); BAC99022, agarase ( Microbulbifer elongatus ); BAB79291, agarase, ( Pseudomonas sp. ND137; AAF21821, β-agarase B precursor ( Zobellia galactanivorans ); AAF21820, β-agarase A precursor ( Zobellia galactanivorans ); AAN39119, extracellular agarase precursor, ( Pseudoalteromonas sp. CY24); CAB61795, extracellular agarase precursor ( Streptomyces coelicolor A3); AAP70364, AguJ (uncultured bacterium); BAA04744, β-agarase ( Vibrio sp.); BAA03541, β-agarase ( Vibrio sp. JT0107); BAH16616, agarase ( Cellvibrio sp. OA-2007); AAT67062, β-agarase I ( Saccharophagus degradans ); AB160954, β-agarase ( Microbulbifer thermotolerans ).

    Article Snippet: Neoagarohexanitol (NA6) was purchased from Sigma (USA) and neoagarotetraose (NA4) and neoagarobiose (NA2) (NA4 + NA2) were prepared by digestion of neoagarohexanitol using commercial β-agarase (New England Biolab, USA).

    Techniques: Sequencing

    The nucleotide and deduced amino acid sequences of the β-agarase of Pseudoalteromonas sp. AG52. The predicted lipoprotein signal peptide is underlined and signal peptide sequence is in bold face. The start (ATG) and stop (TAA) codons are in bold italics and stop codon is marked with an asterisk (*). The GHF-16 β-agarase domain is in italics. Active sites and calcium binding residues are in boxes and dotted boxes, respectively.

    Journal: Brazilian Journal of Microbiology

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    doi: 10.1590/S1517-83822010000400006

    Figure Lengend Snippet: The nucleotide and deduced amino acid sequences of the β-agarase of Pseudoalteromonas sp. AG52. The predicted lipoprotein signal peptide is underlined and signal peptide sequence is in bold face. The start (ATG) and stop (TAA) codons are in bold italics and stop codon is marked with an asterisk (*). The GHF-16 β-agarase domain is in italics. Active sites and calcium binding residues are in boxes and dotted boxes, respectively.

    Article Snippet: Neoagarohexanitol (NA6) was purchased from Sigma (USA) and neoagarotetraose (NA4) and neoagarobiose (NA2) (NA4 + NA2) were prepared by digestion of neoagarohexanitol using commercial β-agarase (New England Biolab, USA).

    Techniques: Sequencing, Binding Assay