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cpu ta1  (InterPro Inc)

 
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    Structured Review

    InterPro Inc cpu ta1
    Transaminase activities.
    Cpu Ta1, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cpu ta1/product/InterPro Inc
    Average 90 stars, based on 1 article reviews
    cpu ta1 - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold"

    Article Title: Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold

    Journal: Scientific Reports

    doi: 10.1038/srep38183

    Transaminase activities.
    Figure Legend Snippet: Transaminase activities.

    Techniques Used: Activity Assay

    Conversions of rac -1-phenylethylamine, rac -1-aminotetralin or rac -1-aminoindane with pyruvate catalysed by the candidate enzymes after 24 h at 30 ° C.
    Figure Legend Snippet: Conversions of rac -1-phenylethylamine, rac -1-aminotetralin or rac -1-aminoindane with pyruvate catalysed by the candidate enzymes after 24 h at 30 ° C.

    Techniques Used:

    Results of transaminase-catalysed amination reactions of pyruvate, α-ketoglutarate, glyoxylic acid, α-keto-γ-(methylthio)-butyrate and phenylpyruvate with rac -1-phenylethylamine, propan-2-amine, rac -butan-2-amine, cyclohexylamine and dl -alanine after 24 h at 30 °C.
    Figure Legend Snippet: Results of transaminase-catalysed amination reactions of pyruvate, α-ketoglutarate, glyoxylic acid, α-keto-γ-(methylthio)-butyrate and phenylpyruvate with rac -1-phenylethylamine, propan-2-amine, rac -butan-2-amine, cyclohexylamine and dl -alanine after 24 h at 30 °C.

    Techniques Used:

    Temperature dependence of specific activities calculated from photometric activity assays using 0.15 mg mL −1 of purified Cpu TA1 ( A ) or 0.1 mg mL −1 of Mgi TA1 ( B ) in 50 mM KPi, pH 8, at various T. The reaction mixtures (5 mM pyruvate, 5 mM ( R )-1-aminotetralin, 0.1 mM PLP in buffer) were incubated for 5 minutes at the respective temperature before addition of pyruvate to start the reaction. The measurements were done in triplicate. Grey diamonds: Cpu TA1, black triangles: Mgi TA1.
    Figure Legend Snippet: Temperature dependence of specific activities calculated from photometric activity assays using 0.15 mg mL −1 of purified Cpu TA1 ( A ) or 0.1 mg mL −1 of Mgi TA1 ( B ) in 50 mM KPi, pH 8, at various T. The reaction mixtures (5 mM pyruvate, 5 mM ( R )-1-aminotetralin, 0.1 mM PLP in buffer) were incubated for 5 minutes at the respective temperature before addition of pyruvate to start the reaction. The measurements were done in triplicate. Grey diamonds: Cpu TA1, black triangles: Mgi TA1.

    Techniques Used: Activity Assay, Purification, Incubation

    ( A ) Overview of the Cpu TA1 dimer (chain A first domain in magenta, second domain in green, chain B in grey); ( B ) Overview of a superposition of the Cpu TA1 dimer (chain A in green, chain B in grey) with the AT-ωTA dimer (Pdb-code: 4CE5, chain A in turquoise, chain B in brown) with the active site cavity of Cpu TA1 depicted as magenta mesh; ( C ) PLP binding amino acids (blue); ( D ) active site amino acids (small binding pocket in yellow, large binding pocket in green); ( E ) entrance tunnel; ( F ) variable loops of Cpu TA1 compared to AT-ωTA. The cavity analysis was calculated by Casox . The figures were prepared using the program PyMOL (Schrodinger Inc.).
    Figure Legend Snippet: ( A ) Overview of the Cpu TA1 dimer (chain A first domain in magenta, second domain in green, chain B in grey); ( B ) Overview of a superposition of the Cpu TA1 dimer (chain A in green, chain B in grey) with the AT-ωTA dimer (Pdb-code: 4CE5, chain A in turquoise, chain B in brown) with the active site cavity of Cpu TA1 depicted as magenta mesh; ( C ) PLP binding amino acids (blue); ( D ) active site amino acids (small binding pocket in yellow, large binding pocket in green); ( E ) entrance tunnel; ( F ) variable loops of Cpu TA1 compared to AT-ωTA. The cavity analysis was calculated by Casox . The figures were prepared using the program PyMOL (Schrodinger Inc.).

    Techniques Used: Binding Assay



    Similar Products

    cpu ta1  (InterPro Inc)
    90
    InterPro Inc cpu ta1
    Transaminase activities.
    Cpu Ta1, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cpu ta1/product/InterPro Inc
    Average 90 stars, based on 1 article reviews
    cpu ta1 - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Transaminase activities.

    Journal: Scientific Reports

    Article Title: Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold

    doi: 10.1038/srep38183

    Figure Lengend Snippet: Transaminase activities.

    Article Snippet: Cpu TA1 exhibits the typical aminotransferase type IV fold (InterPro: IPR001544, Pfam: Pf01063).

    Techniques: Activity Assay

    Conversions of rac -1-phenylethylamine, rac -1-aminotetralin or rac -1-aminoindane with pyruvate catalysed by the candidate enzymes after 24 h at 30 ° C.

    Journal: Scientific Reports

    Article Title: Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold

    doi: 10.1038/srep38183

    Figure Lengend Snippet: Conversions of rac -1-phenylethylamine, rac -1-aminotetralin or rac -1-aminoindane with pyruvate catalysed by the candidate enzymes after 24 h at 30 ° C.

    Article Snippet: Cpu TA1 exhibits the typical aminotransferase type IV fold (InterPro: IPR001544, Pfam: Pf01063).

    Techniques:

    Results of transaminase-catalysed amination reactions of pyruvate, α-ketoglutarate, glyoxylic acid, α-keto-γ-(methylthio)-butyrate and phenylpyruvate with rac -1-phenylethylamine, propan-2-amine, rac -butan-2-amine, cyclohexylamine and dl -alanine after 24 h at 30 °C.

    Journal: Scientific Reports

    Article Title: Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold

    doi: 10.1038/srep38183

    Figure Lengend Snippet: Results of transaminase-catalysed amination reactions of pyruvate, α-ketoglutarate, glyoxylic acid, α-keto-γ-(methylthio)-butyrate and phenylpyruvate with rac -1-phenylethylamine, propan-2-amine, rac -butan-2-amine, cyclohexylamine and dl -alanine after 24 h at 30 °C.

    Article Snippet: Cpu TA1 exhibits the typical aminotransferase type IV fold (InterPro: IPR001544, Pfam: Pf01063).

    Techniques:

    Temperature dependence of specific activities calculated from photometric activity assays using 0.15 mg mL −1 of purified Cpu TA1 ( A ) or 0.1 mg mL −1 of Mgi TA1 ( B ) in 50 mM KPi, pH 8, at various T. The reaction mixtures (5 mM pyruvate, 5 mM ( R )-1-aminotetralin, 0.1 mM PLP in buffer) were incubated for 5 minutes at the respective temperature before addition of pyruvate to start the reaction. The measurements were done in triplicate. Grey diamonds: Cpu TA1, black triangles: Mgi TA1.

    Journal: Scientific Reports

    Article Title: Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold

    doi: 10.1038/srep38183

    Figure Lengend Snippet: Temperature dependence of specific activities calculated from photometric activity assays using 0.15 mg mL −1 of purified Cpu TA1 ( A ) or 0.1 mg mL −1 of Mgi TA1 ( B ) in 50 mM KPi, pH 8, at various T. The reaction mixtures (5 mM pyruvate, 5 mM ( R )-1-aminotetralin, 0.1 mM PLP in buffer) were incubated for 5 minutes at the respective temperature before addition of pyruvate to start the reaction. The measurements were done in triplicate. Grey diamonds: Cpu TA1, black triangles: Mgi TA1.

    Article Snippet: Cpu TA1 exhibits the typical aminotransferase type IV fold (InterPro: IPR001544, Pfam: Pf01063).

    Techniques: Activity Assay, Purification, Incubation

    ( A ) Overview of the Cpu TA1 dimer (chain A first domain in magenta, second domain in green, chain B in grey); ( B ) Overview of a superposition of the Cpu TA1 dimer (chain A in green, chain B in grey) with the AT-ωTA dimer (Pdb-code: 4CE5, chain A in turquoise, chain B in brown) with the active site cavity of Cpu TA1 depicted as magenta mesh; ( C ) PLP binding amino acids (blue); ( D ) active site amino acids (small binding pocket in yellow, large binding pocket in green); ( E ) entrance tunnel; ( F ) variable loops of Cpu TA1 compared to AT-ωTA. The cavity analysis was calculated by Casox . The figures were prepared using the program PyMOL (Schrodinger Inc.).

    Journal: Scientific Reports

    Article Title: Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold

    doi: 10.1038/srep38183

    Figure Lengend Snippet: ( A ) Overview of the Cpu TA1 dimer (chain A first domain in magenta, second domain in green, chain B in grey); ( B ) Overview of a superposition of the Cpu TA1 dimer (chain A in green, chain B in grey) with the AT-ωTA dimer (Pdb-code: 4CE5, chain A in turquoise, chain B in brown) with the active site cavity of Cpu TA1 depicted as magenta mesh; ( C ) PLP binding amino acids (blue); ( D ) active site amino acids (small binding pocket in yellow, large binding pocket in green); ( E ) entrance tunnel; ( F ) variable loops of Cpu TA1 compared to AT-ωTA. The cavity analysis was calculated by Casox . The figures were prepared using the program PyMOL (Schrodinger Inc.).

    Article Snippet: Cpu TA1 exhibits the typical aminotransferase type IV fold (InterPro: IPR001544, Pfam: Pf01063).

    Techniques: Binding Assay