p putida kt2440  (ATCC)


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    ATCC p putida kt2440
    P Putida Kt2440, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pseudomonas putida trevisan migula mnb1  (ATCC)


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    ATCC pseudomonas putida trevisan migula mnb1
    Comparison of the theoretical structure of CumA from Pseudomonas <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula Mnb1, supplied by ATCC, 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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    1) Product Images from "Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation"

    Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation

    Journal: Life

    doi: 10.3390/life14020171

    Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Figure Legend Snippet: Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.

    Techniques Used: Comparison, Sequencing

    Composition of whole-cell BMO from  MnB1  and acid birnessite via ICP-OES. Samples were dissolved in concentrated HCl and tested for manganese, calcium, potassium, magnesium, iron, copper, and zinc.
    Figure Legend Snippet: Composition of whole-cell BMO from MnB1 and acid birnessite via ICP-OES. Samples were dissolved in concentrated HCl and tested for manganese, calcium, potassium, magnesium, iron, copper, and zinc.

    Techniques Used:

    Powder X-ray diffraction patterns of whole-cell BMO from MnB1 and acid birnessite samples. The XRD pattern of a layered Mn oxide, birnessite (Crystallography Open Database ID entry: 9013650), is provided for reference.
    Figure Legend Snippet: Powder X-ray diffraction patterns of whole-cell BMO from MnB1 and acid birnessite samples. The XRD pattern of a layered Mn oxide, birnessite (Crystallography Open Database ID entry: 9013650), is provided for reference.

    Techniques Used:

    p putida kt2440  (ATCC)


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    ATCC p putida kt2440
    P Putida Kt2440, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    soil bacterium pseudomonas putida kt2440  (ATCC)


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    ATCC soil bacterium pseudomonas putida kt2440
    Effects of exogenous application of root exudate compounds (oxalic acid, glucose, shikimic acid, p -coumaric acid) on ( A ) growth of Pseudomonas putida <t>KT2440</t> ( c = 5, 50, and 500 µM) in a multiwell plate and ( B ) 3 days old Brachypodium distachyon Bd21-3 seedlings ( c = 500 µM) on phytoagar plates. ( A ) Shikimic acid increased microbial growth. ( B ) Shikimic acid increased root length under iN supply, while oxalic and p -coumaric acid decreased root length under iN starvation. The p -coumaric acid significantly decreased shoot length independent of iN supply. The iN was supplied at 2.5 mM of NH 4 NO 3 . Different letters indicate statistically significant differences (two-way ANOVA with post hoc Tukey’s HSD test; n = 48; p ≤ 0.05). The right panel shows representative seedlings’ phenotypes at day 3 since the onset of germination in the presence of the compounds. Arrows point to root areas with localized high root hair density in oxalic and p -coumaric acid treatments. All seedling pictures in high resolution are available at https://doi.org/10.6084/m9.figshare.21433065 .
    Soil Bacterium Pseudomonas Putida Kt2440, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Reproducible growth of Brachypodium distachyon in fabricated ecosystems (EcoFAB 2.0) reveals that nitrogen form and starvation modulate root exudation"

    Article Title: Reproducible growth of Brachypodium distachyon in fabricated ecosystems (EcoFAB 2.0) reveals that nitrogen form and starvation modulate root exudation

    Journal: bioRxiv

    doi: 10.1101/2023.01.18.524647

    Effects of exogenous application of root exudate compounds (oxalic acid, glucose, shikimic acid, p -coumaric acid) on ( A ) growth of Pseudomonas putida KT2440 ( c = 5, 50, and 500 µM) in a multiwell plate and ( B ) 3 days old Brachypodium distachyon Bd21-3 seedlings ( c = 500 µM) on phytoagar plates. ( A ) Shikimic acid increased microbial growth. ( B ) Shikimic acid increased root length under iN supply, while oxalic and p -coumaric acid decreased root length under iN starvation. The p -coumaric acid significantly decreased shoot length independent of iN supply. The iN was supplied at 2.5 mM of NH 4 NO 3 . Different letters indicate statistically significant differences (two-way ANOVA with post hoc Tukey’s HSD test; n = 48; p ≤ 0.05). The right panel shows representative seedlings’ phenotypes at day 3 since the onset of germination in the presence of the compounds. Arrows point to root areas with localized high root hair density in oxalic and p -coumaric acid treatments. All seedling pictures in high resolution are available at https://doi.org/10.6084/m9.figshare.21433065 .
    Figure Legend Snippet: Effects of exogenous application of root exudate compounds (oxalic acid, glucose, shikimic acid, p -coumaric acid) on ( A ) growth of Pseudomonas putida KT2440 ( c = 5, 50, and 500 µM) in a multiwell plate and ( B ) 3 days old Brachypodium distachyon Bd21-3 seedlings ( c = 500 µM) on phytoagar plates. ( A ) Shikimic acid increased microbial growth. ( B ) Shikimic acid increased root length under iN supply, while oxalic and p -coumaric acid decreased root length under iN starvation. The p -coumaric acid significantly decreased shoot length independent of iN supply. The iN was supplied at 2.5 mM of NH 4 NO 3 . Different letters indicate statistically significant differences (two-way ANOVA with post hoc Tukey’s HSD test; n = 48; p ≤ 0.05). The right panel shows representative seedlings’ phenotypes at day 3 since the onset of germination in the presence of the compounds. Arrows point to root areas with localized high root hair density in oxalic and p -coumaric acid treatments. All seedling pictures in high resolution are available at https://doi.org/10.6084/m9.figshare.21433065 .

    Techniques Used:

    p putida atcc 17453  (ATCC)


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    ATCC p putida atcc 17453
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    P Putida Atcc 17453, supplied by ATCC, 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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    1) Product Images from "Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations"

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    Journal: Microorganisms

    doi: 10.3390/microorganisms11010071

    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    Figure Legend Snippet: The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Techniques Used:

    Calculated apparent Km FMN values for highly purified representative FRs from  P. putida ATCC 17453  and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ <xref ref-type= 35 ] and 1.0 μM [ 40 ], respectively." title="... FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Calculated apparent Km FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ 35 ] and 1.0 μM [ 40 ], respectively.

    Techniques Used: Purification, Luciferase

    p putida atcc 17453  (ATCC)


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    ATCC p putida atcc 17453
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    P Putida Atcc 17453, supplied by ATCC, 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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    1) Product Images from "Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations"

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    Journal: Microorganisms

    doi: 10.3390/microorganisms11010071

    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    Figure Legend Snippet: The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Techniques Used:

    Calculated apparent Km FMN values for highly purified representative FRs from  P. putida ATCC 17453  and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ <xref ref-type= 35 ] and 1.0 μM [ 40 ], respectively." title="... FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Calculated apparent Km FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ 35 ] and 1.0 μM [ 40 ], respectively.

    Techniques Used: Purification, Luciferase

    pseudomonas putida trevisan migula  (ATCC)


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    ATCC pseudomonas putida trevisan migula
    Pseudomonas Putida Trevisan Migula, supplied by ATCC, 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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    p putida atcc 17453  (ATCC)


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    ATCC p putida atcc 17453
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    P Putida Atcc 17453, supplied by ATCC, 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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    1) Product Images from "Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations"

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    Journal: Microorganisms

    doi: 10.3390/microorganisms11010071

    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    Figure Legend Snippet: The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Techniques Used:

    Calculated apparent Km FMN values for highly purified representative FRs from  P. putida ATCC 17453  and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ <xref ref-type= 35 ] and 1.0 μM [ 40 ], respectively." title="... FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Calculated apparent Km FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ 35 ] and 1.0 μM [ 40 ], respectively.

    Techniques Used: Purification, Luciferase

    p putida atcc 17453  (ATCC)


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    ATCC p putida atcc 17453
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    P Putida Atcc 17453, supplied by ATCC, 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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    1) Product Images from "Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations"

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    Journal: Microorganisms

    doi: 10.3390/microorganisms11010071

    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    Figure Legend Snippet: The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Techniques Used:

    Calculated apparent Km FMN values for highly purified representative FRs from  P. putida ATCC 17453  and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ <xref ref-type= 35 ] and 1.0 μM [ 40 ], respectively." title="... FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Calculated apparent Km FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ 35 ] and 1.0 μM [ 40 ], respectively.

    Techniques Used: Purification, Luciferase

    p putida atcc 17453  (ATCC)


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    ATCC p putida atcc 17453
    Characterised FMN-dependent FRs [ <xref ref-type= 5 ]." width="250" height="auto" />
    P Putida Atcc 17453, supplied by ATCC, 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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    1) Product Images from "Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations"

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    Journal: Microorganisms

    doi: 10.3390/microorganisms11010071

    Characterised FMN-dependent FRs [ <xref ref-type= 5 ]." title=" Characterised FMN-dependent FRs [5]. " property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Characterised FMN-dependent FRs [ 5 ].

    Techniques Used:

    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    Figure Legend Snippet: The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Techniques Used:

    Calculated apparent Km FMN values for highly purified representative FRs from  P. putida ATCC 17453  and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ <xref ref-type= 35 ] and 1.0 μM [ 40 ], respectively." title="... FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Calculated apparent Km FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ 35 ] and 1.0 μM [ 40 ], respectively.

    Techniques Used: Purification, Luciferase

    Potential outcomes for the biooxygenation of ( rac )-bicyclo-[3.2.0]hept-2-en-6-one to 2-oxa- and 3-oxa-lactones by fd-TCMOs dependent on FMNH 2 sourced from an FR. Tested fd-TCMOs: 2,5-DKCMO; 3,6-DKCMO; LuxAB luciferase. Tested FRs: Frp1 ( P. putida ); Frp2 ( P. putida ); Fre Vf ( V. fischeri ); FRG Vf ( V. fischeri ); Fre Ec ( E. coli ); FRD Aa ( A. aminovorans ).
    Figure Legend Snippet: Potential outcomes for the biooxygenation of ( rac )-bicyclo-[3.2.0]hept-2-en-6-one to 2-oxa- and 3-oxa-lactones by fd-TCMOs dependent on FMNH 2 sourced from an FR. Tested fd-TCMOs: 2,5-DKCMO; 3,6-DKCMO; LuxAB luciferase. Tested FRs: Frp1 ( P. putida ); Frp2 ( P. putida ); Fre Vf ( V. fischeri ); FRG Vf ( V. fischeri ); Fre Ec ( E. coli ); FRD Aa ( A. aminovorans ).

    Techniques Used: Luciferase

    120 min outcomes of the fd-TCMO-FR coupled-enzyme reactions with highly purified preparations of LuxAB luciferase , 2,5-DKCMO , and 3,6-DKCMO with FRs from P. putida (Frp1 and  Frp2),  V. fischeri (FRG Vf and Fre Vf ), A. aminovorans (FRD Aa ) and E. coli (Fre Ec ). The structures of (+)k, (−)k, (+)2l, (−)2l, (+)3l, and (−)3l are shown in <xref ref-type= Figure 2 . (n) = native FR, (n.n) = non-native FR." title="... 3,6-DKCMO with FRs from P. putida (Frp1 and Frp2), V. fischeri (FRG Vf and Fre ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: 120 min outcomes of the fd-TCMO-FR coupled-enzyme reactions with highly purified preparations of LuxAB luciferase , 2,5-DKCMO , and 3,6-DKCMO with FRs from P. putida (Frp1 and Frp2), V. fischeri (FRG Vf and Fre Vf ), A. aminovorans (FRD Aa ) and E. coli (Fre Ec ). The structures of (+)k, (−)k, (+)2l, (−)2l, (+)3l, and (−)3l are shown in Figure 2 . (n) = native FR, (n.n) = non-native FR.

    Techniques Used: Purification, Luciferase

    putidaredoxin reductase pdr  (ATCC)


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    Structured Review

    ATCC putidaredoxin reductase pdr
    Putidaredoxin Reductase Pdr, supplied by ATCC, 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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    ATCC p putida kt2440
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    ATCC pseudomonas putida trevisan migula mnb1
    Comparison of the theoretical structure of CumA from Pseudomonas <t>putida</t> and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.
    Pseudomonas Putida Trevisan Migula Mnb1, supplied by ATCC, 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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    ATCC soil bacterium pseudomonas putida kt2440
    Effects of exogenous application of root exudate compounds (oxalic acid, glucose, shikimic acid, p -coumaric acid) on ( A ) growth of Pseudomonas putida <t>KT2440</t> ( c = 5, 50, and 500 µM) in a multiwell plate and ( B ) 3 days old Brachypodium distachyon Bd21-3 seedlings ( c = 500 µM) on phytoagar plates. ( A ) Shikimic acid increased microbial growth. ( B ) Shikimic acid increased root length under iN supply, while oxalic and p -coumaric acid decreased root length under iN starvation. The p -coumaric acid significantly decreased shoot length independent of iN supply. The iN was supplied at 2.5 mM of NH 4 NO 3 . Different letters indicate statistically significant differences (two-way ANOVA with post hoc Tukey’s HSD test; n = 48; p ≤ 0.05). The right panel shows representative seedlings’ phenotypes at day 3 since the onset of germination in the presence of the compounds. Arrows point to root areas with localized high root hair density in oxalic and p -coumaric acid treatments. All seedling pictures in high resolution are available at https://doi.org/10.6084/m9.figshare.21433065 .
    Soil Bacterium Pseudomonas Putida Kt2440, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC p putida atcc 17453
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    P Putida Atcc 17453, supplied by ATCC, 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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    ATCC pseudomonas putida trevisan migula
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
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    ATCC putidaredoxin reductase pdr
    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .
    Putidaredoxin Reductase Pdr, supplied by ATCC, 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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    Image Search Results


    Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.

    Journal: Life

    Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation

    doi: 10.3390/life14020171

    Figure Lengend Snippet: Comparison of the theoretical structure of CumA from Pseudomonas putida and other well-studied multi-copper oxidases . ( A ) Proposed structure of CumA determined in AlphaFold [ , ]; ( B ) overlay of the calculated structure of CumA and Laccase from Bacillus subtilis; ( C ) active site of Laccase; ( D ) protein sequence alignments of CumA (unknown structure). CueO a Mn(II)-oxidizing multi-copper oxidase from Escherichia coli strain K12 and Laccase. (*) indicates conserved amino acids, (:) indicates semi-conserved residues, (.) indicates an evolutionary divergence of residues. Letter colors indicate the type of amino acid: green (polar), red (nonpolar), blue (acidic), and pink (basic). Red boxes highlight the active sites that bind copper ions and are conserved in all multi-copper oxidases.

    Article Snippet: Cultures of Pseudomonas putida (Trevisan) Migula MnB1 supplied by American Type Culture Collection (ATCC #23483) were prepared and grown at room temperature or 30 °C for 3 days.

    Techniques: Comparison, Sequencing

    Composition of whole-cell BMO from  MnB1  and acid birnessite via ICP-OES. Samples were dissolved in concentrated HCl and tested for manganese, calcium, potassium, magnesium, iron, copper, and zinc.

    Journal: Life

    Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation

    doi: 10.3390/life14020171

    Figure Lengend Snippet: Composition of whole-cell BMO from MnB1 and acid birnessite via ICP-OES. Samples were dissolved in concentrated HCl and tested for manganese, calcium, potassium, magnesium, iron, copper, and zinc.

    Article Snippet: Cultures of Pseudomonas putida (Trevisan) Migula MnB1 supplied by American Type Culture Collection (ATCC #23483) were prepared and grown at room temperature or 30 °C for 3 days.

    Techniques:

    Powder X-ray diffraction patterns of whole-cell BMO from MnB1 and acid birnessite samples. The XRD pattern of a layered Mn oxide, birnessite (Crystallography Open Database ID entry: 9013650), is provided for reference.

    Journal: Life

    Article Title: Characterizing Biogenic MnOx Produced by Pseudomonas putida MnB1 and Its Catalytic Activity towards Water Oxidation

    doi: 10.3390/life14020171

    Figure Lengend Snippet: Powder X-ray diffraction patterns of whole-cell BMO from MnB1 and acid birnessite samples. The XRD pattern of a layered Mn oxide, birnessite (Crystallography Open Database ID entry: 9013650), is provided for reference.

    Article Snippet: Cultures of Pseudomonas putida (Trevisan) Migula MnB1 supplied by American Type Culture Collection (ATCC #23483) were prepared and grown at room temperature or 30 °C for 3 days.

    Techniques:

    Effects of exogenous application of root exudate compounds (oxalic acid, glucose, shikimic acid, p -coumaric acid) on ( A ) growth of Pseudomonas putida KT2440 ( c = 5, 50, and 500 µM) in a multiwell plate and ( B ) 3 days old Brachypodium distachyon Bd21-3 seedlings ( c = 500 µM) on phytoagar plates. ( A ) Shikimic acid increased microbial growth. ( B ) Shikimic acid increased root length under iN supply, while oxalic and p -coumaric acid decreased root length under iN starvation. The p -coumaric acid significantly decreased shoot length independent of iN supply. The iN was supplied at 2.5 mM of NH 4 NO 3 . Different letters indicate statistically significant differences (two-way ANOVA with post hoc Tukey’s HSD test; n = 48; p ≤ 0.05). The right panel shows representative seedlings’ phenotypes at day 3 since the onset of germination in the presence of the compounds. Arrows point to root areas with localized high root hair density in oxalic and p -coumaric acid treatments. All seedling pictures in high resolution are available at https://doi.org/10.6084/m9.figshare.21433065 .

    Journal: bioRxiv

    Article Title: Reproducible growth of Brachypodium distachyon in fabricated ecosystems (EcoFAB 2.0) reveals that nitrogen form and starvation modulate root exudation

    doi: 10.1101/2023.01.18.524647

    Figure Lengend Snippet: Effects of exogenous application of root exudate compounds (oxalic acid, glucose, shikimic acid, p -coumaric acid) on ( A ) growth of Pseudomonas putida KT2440 ( c = 5, 50, and 500 µM) in a multiwell plate and ( B ) 3 days old Brachypodium distachyon Bd21-3 seedlings ( c = 500 µM) on phytoagar plates. ( A ) Shikimic acid increased microbial growth. ( B ) Shikimic acid increased root length under iN supply, while oxalic and p -coumaric acid decreased root length under iN starvation. The p -coumaric acid significantly decreased shoot length independent of iN supply. The iN was supplied at 2.5 mM of NH 4 NO 3 . Different letters indicate statistically significant differences (two-way ANOVA with post hoc Tukey’s HSD test; n = 48; p ≤ 0.05). The right panel shows representative seedlings’ phenotypes at day 3 since the onset of germination in the presence of the compounds. Arrows point to root areas with localized high root hair density in oxalic and p -coumaric acid treatments. All seedling pictures in high resolution are available at https://doi.org/10.6084/m9.figshare.21433065 .

    Article Snippet: We selected representative compounds from shikimate (shikimic acid) and phenylpropanoid ( p -coumaric acid) pathways to test their impact on the growth of soil bacterium Pseudomonas putida KT2440 (ATCC 47054), which was shown to colonize plant roots ( ).

    Techniques:

    The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Journal: Microorganisms

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    doi: 10.3390/microorganisms11010071

    Figure Lengend Snippet: The different types (bound vs. unbound flavin) and the different reaction mechanisms (sequential vs. ping-pong) of the flavin reductases of V. fischeri ATCC 7744 and P. putida ATCC 17453. E = flavin reductase with unbound flavin coenzyme (Frp1; Frp2; Fred; Fre Vf ): F = FMN: EF* = flavin reductase with bound flavin coenzyme (FRG Vf [FMN]; PdR [FAD]): FH 2 = FMNH 2 .

    Article Snippet: Because the (−)-( 1S , 5R )-2-oxa-lactone formed is an acknowledged synthon for the chemoenzymatic synthesis of various potentially useful prostaglandin analogues [ ], it is significant that the calculated enantiomeric purities [ ] of the (−)-2-oxa-lactone recorded with this monooxygenase in combination with each of the tested purified FRs are all higher than those reported previously for equivalent biotransformations undertaken by the Type 1 BVMOs 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase sourced from P. putida ATCC 17453 [ , , ], and cyclohexanone monooxygenase sourced from either Acinetobacter TD63 [ ], or Acinetobacter calcoaceticus NCIMB 9871 [ , ].

    Techniques:

    Calculated apparent Km FMN values for highly purified representative FRs from  P. putida ATCC 17453  and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ <xref ref-type= 35 ] and 1.0 μM [ 40 ], respectively." width="100%" height="100%">

    Journal: Microorganisms

    Article Title: Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer–Villiger Biooxygenations

    doi: 10.3390/microorganisms11010071

    Figure Lengend Snippet: Calculated apparent Km FMN values for highly purified representative FRs from P. putida ATCC 17453 and V. fischeri ATCC 7744 tested both as single-enzyme assays (S) and coupled-enzyme assays with 2,5-DKCMO (C:+ 2,5-MO ), 3,6-DKCMO (C :+3,6-MO ), and LuxAB luciferase (C:+ LuxAB ) and, in each case, 1mM of the biooxidisable ketone ( rac )-bicyclo[3.2.0]hept-2-en-6-one. The equivalent reported single-enzyme Km FMN values for Fre Ec and FRD Aa are 0.8 μM [ 35 ] and 1.0 μM [ 40 ], respectively.

    Article Snippet: Because the (−)-( 1S , 5R )-2-oxa-lactone formed is an acknowledged synthon for the chemoenzymatic synthesis of various potentially useful prostaglandin analogues [ ], it is significant that the calculated enantiomeric purities [ ] of the (−)-2-oxa-lactone recorded with this monooxygenase in combination with each of the tested purified FRs are all higher than those reported previously for equivalent biotransformations undertaken by the Type 1 BVMOs 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase sourced from P. putida ATCC 17453 [ , , ], and cyclohexanone monooxygenase sourced from either Acinetobacter TD63 [ ], or Acinetobacter calcoaceticus NCIMB 9871 [ , ].

    Techniques: Purification, Luciferase