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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    Images

    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 atcc 17453  (ATCC)


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    ATCC pseudomonas putida atcc 17453
    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.
    Pseudomonas Putida Atcc 17453, 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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    Images

    1) Product Images from "The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme"

    Article Title: The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme

    Journal: Microorganisms

    doi: 10.3390/microorganisms12020389

    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.
    Figure Legend Snippet: CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.

    Techniques Used: Plasmid Preparation

    ( A , B ) The two representations developed by Gunsalus [  ,  ,  ,  ,  ,  ] to explain the functional interaction of NADH oxidase and 2,5-diketocamphane monooxygenase in undertaking O 2 -dependent lactonization of 2,5-diketocamphane in camphor-grown Pseudomonas putida ATCC 17453. E 1 = NADH oxidase; E 2 = 2,5-diketocamphane monooxygenase; MB = methylene blue; DKC = 2,5-diketocamphane.
    Figure Legend Snippet: ( A , B ) The two representations developed by Gunsalus [ , , , , , ] to explain the functional interaction of NADH oxidase and 2,5-diketocamphane monooxygenase in undertaking O 2 -dependent lactonization of 2,5-diketocamphane in camphor-grown Pseudomonas putida ATCC 17453. E 1 = NADH oxidase; E 2 = 2,5-diketocamphane monooxygenase; MB = methylene blue; DKC = 2,5-diketocamphane.

    Techniques Used: Functional Assay

    Schematic of the two contrasting roles of putidaredoxin reductase (PR) in camphor-grown P. putida ATCC 17453. Reaction 1 is common to both roles. In both cases, the sequence of reactions progresses from one to three. P450MO = cytochrome P450 mono-oxygenase; Pdx = putidaredoxin; DKCMO = 2,5-diketocamphane 1,2-mono-oxygenase; DKC = 2,5-diketocamphane.
    Figure Legend Snippet: Schematic of the two contrasting roles of putidaredoxin reductase (PR) in camphor-grown P. putida ATCC 17453. Reaction 1 is common to both roles. In both cases, the sequence of reactions progresses from one to three. P450MO = cytochrome P450 mono-oxygenase; Pdx = putidaredoxin; DKCMO = 2,5-diketocamphane 1,2-mono-oxygenase; DKC = 2,5-diketocamphane.

    Techniques Used: Sequencing

    pseudomonas putida atcc 17453  (ATCC)


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    ATCC pseudomonas putida atcc 17453
    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.
    Pseudomonas Putida Atcc 17453, 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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    Images

    1) Product Images from "The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme"

    Article Title: The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme

    Journal: Microorganisms

    doi: 10.3390/microorganisms12020389

    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.
    Figure Legend Snippet: CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.

    Techniques Used: Plasmid Preparation

    ( A , B ) The two representations developed by Gunsalus [  ,  ,  ,  ,  ,  ] to explain the functional interaction of NADH oxidase and 2,5-diketocamphane monooxygenase in undertaking O 2 -dependent lactonization of 2,5-diketocamphane in camphor-grown Pseudomonas putida ATCC 17453. E 1 = NADH oxidase; E 2 = 2,5-diketocamphane monooxygenase; MB = methylene blue; DKC = 2,5-diketocamphane.
    Figure Legend Snippet: ( A , B ) The two representations developed by Gunsalus [ , , , , , ] to explain the functional interaction of NADH oxidase and 2,5-diketocamphane monooxygenase in undertaking O 2 -dependent lactonization of 2,5-diketocamphane in camphor-grown Pseudomonas putida ATCC 17453. E 1 = NADH oxidase; E 2 = 2,5-diketocamphane monooxygenase; MB = methylene blue; DKC = 2,5-diketocamphane.

    Techniques Used: Functional Assay

    Schematic of the two contrasting roles of putidaredoxin reductase (PR) in camphor-grown P. putida ATCC 17453. Reaction 1 is common to both roles. In both cases, the sequence of reactions progresses from one to three. P450MO = cytochrome P450 mono-oxygenase; Pdx = putidaredoxin; DKCMO = 2,5-diketocamphane 1,2-mono-oxygenase; DKC = 2,5-diketocamphane.
    Figure Legend Snippet: Schematic of the two contrasting roles of putidaredoxin reductase (PR) in camphor-grown P. putida ATCC 17453. Reaction 1 is common to both roles. In both cases, the sequence of reactions progresses from one to three. P450MO = cytochrome P450 mono-oxygenase; Pdx = putidaredoxin; DKCMO = 2,5-diketocamphane 1,2-mono-oxygenase; DKC = 2,5-diketocamphane.

    Techniques Used: Sequencing

    pseudomonas putida strain atcc 17453  (ATCC)


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    ATCC pseudomonas putida strain atcc 17453
    Pseudomonas Putida Strain Atcc 17453, 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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    pseudomonas putida atcc 17453  (ATCC)


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    ATCC pseudomonas putida atcc 17453
    Pseudomonas Putida Atcc 17453, 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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    pseudomonas putida atcc 17453  (ATCC)


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    ATCC pseudomonas putida atcc 17453
    Pseudomonas Putida Atcc 17453, 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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    pseudomonas putida atcc 17453  (ATCC)


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    ATCC pseudomonas putida atcc 17453
    Pseudomonas Putida Atcc 17453, 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
    https://www.bioz.com/result/p putida atcc 17453/product/ATCC
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p putida atcc 17453 - by Bioz Stars, 2024-05
    95/100 stars

    Images

    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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    Images

    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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    95/100 stars

    Images

    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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    Structured Review

    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
    https://www.bioz.com/result/p putida atcc 17453/product/ATCC
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p putida atcc 17453 - by Bioz Stars, 2024-05
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    Images

    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

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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
    https://www.bioz.com/result/p putida atcc 17453/product/ATCC
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    Price from $9.99 to $1999.99
    p putida atcc 17453 - by Bioz Stars, 2024-05
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    86
    ATCC pseudomonas putida atcc 17453
    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.
    Pseudomonas Putida Atcc 17453, 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 pseudomonas putida strain atcc 17453
    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.
    Pseudomonas Putida Strain Atcc 17453, 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
    https://www.bioz.com/result/pseudomonas putida strain atcc 17453/product/ATCC
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    Image Search Results


    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

    CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.

    Journal: Microorganisms

    Article Title: The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme

    doi: 10.3390/microorganisms12020389

    Figure Lengend Snippet: CAM plasmid-coded pathway of ( rac )-camphor degradation by Pseudomonas putida ATCC 17453: adapted from . a = cytochrome P450 monooxygenase ( camCAB ); b = hydroxycamphor dehydrogenase ( camD ); c = 2,5-diketocamphane 1,2-monooxygenase ( camE 25-1 + camE 25-2 ); d = 3,6-diketocamphane 1,6-monooxygenase ( camE 36 ); e = 2-oxo-Δ 3 -4,5,5,-trimethylcyclopentenylacetyl-CoA monooxygenase ( camG ); (+)-1 and (-)-1 = ( R )- and ( S )-enantiomers of camphor, respectively; 2a = 2,5-diketocamphane; 2b = 3,6-diketocamphane; 3 = 2-oxo-Δ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA; 4 = 3,4,4-trimethyl-Δ 2 -pimelyl-CoA lactone.

    Article Snippet: A useful insight into this can be gained by reviewing the evolution of the current status of 2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108) from (+)-camphor-grown Pseudomonas putida ATCC 17453, the key enzyme that promotes the initial ring cleavage of this natural bicyclic terpene.

    Techniques: Plasmid Preparation

    ( A , B ) The two representations developed by Gunsalus [  ,  ,  ,  ,  ,  ] to explain the functional interaction of NADH oxidase and 2,5-diketocamphane monooxygenase in undertaking O 2 -dependent lactonization of 2,5-diketocamphane in camphor-grown Pseudomonas putida ATCC 17453. E 1 = NADH oxidase; E 2 = 2,5-diketocamphane monooxygenase; MB = methylene blue; DKC = 2,5-diketocamphane.

    Journal: Microorganisms

    Article Title: The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme

    doi: 10.3390/microorganisms12020389

    Figure Lengend Snippet: ( A , B ) The two representations developed by Gunsalus [ , , , , , ] to explain the functional interaction of NADH oxidase and 2,5-diketocamphane monooxygenase in undertaking O 2 -dependent lactonization of 2,5-diketocamphane in camphor-grown Pseudomonas putida ATCC 17453. E 1 = NADH oxidase; E 2 = 2,5-diketocamphane monooxygenase; MB = methylene blue; DKC = 2,5-diketocamphane.

    Article Snippet: A useful insight into this can be gained by reviewing the evolution of the current status of 2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108) from (+)-camphor-grown Pseudomonas putida ATCC 17453, the key enzyme that promotes the initial ring cleavage of this natural bicyclic terpene.

    Techniques: Functional Assay

    Schematic of the two contrasting roles of putidaredoxin reductase (PR) in camphor-grown P. putida ATCC 17453. Reaction 1 is common to both roles. In both cases, the sequence of reactions progresses from one to three. P450MO = cytochrome P450 mono-oxygenase; Pdx = putidaredoxin; DKCMO = 2,5-diketocamphane 1,2-mono-oxygenase; DKC = 2,5-diketocamphane.

    Journal: Microorganisms

    Article Title: The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme

    doi: 10.3390/microorganisms12020389

    Figure Lengend Snippet: Schematic of the two contrasting roles of putidaredoxin reductase (PR) in camphor-grown P. putida ATCC 17453. Reaction 1 is common to both roles. In both cases, the sequence of reactions progresses from one to three. P450MO = cytochrome P450 mono-oxygenase; Pdx = putidaredoxin; DKCMO = 2,5-diketocamphane 1,2-mono-oxygenase; DKC = 2,5-diketocamphane.

    Article Snippet: A useful insight into this can be gained by reviewing the evolution of the current status of 2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108) from (+)-camphor-grown Pseudomonas putida ATCC 17453, the key enzyme that promotes the initial ring cleavage of this natural bicyclic terpene.

    Techniques: Sequencing