PUBLICACIÓN

Rat liver nucleotide pyrophosphatase/phosphodiesterase is an efficient adenylyl transferase

ACCEDER A LA PUBLICACIÓN: Scopus Orcid

Ribeiro, J.M., López-Gómez, J., Vergeles, J.M., Costas, M.J., García-Díaz, M., Fernández, A., Flores, A., Cameselle, J.C.

2000 Biochemical Journal

CITAS

4

DOI

10.1042/0264-6021:3460025

EID

2-s2.0-0034652306

ISSN

0264-6021

BIBTEX

@article{Ribeiro2000,title = {Rat liver nucleotide pyrophosphatase/phosphodiesterase is an efficient adenylyl transferase},journal = {Biochemical Journal},year = {2000},volume = {346},number = {1},pages = {25-31},author = {Ribeiro, J.M. and L{\'o}pez-G{\'o}mez, J. and Vergeles, J.M. and Costas, M.J. and Garc{\'i}a-D{\'i}az, M. and Fern{\'a}ndez, A. and Flores, A. and Cameselle, J.C.}}

AUTORES DE LA UEX

Juan Nuno Meireles Da Silva Gonçalves Ribeiro

OTRAS PUBLICACIONES DE INTERÉS

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Homozygous Variant In Tkfc Abolishing Triokinase Activities Is Associated With Isolated Immunodeficiency
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase / Phosphodiesterase Enpp3 Elicited By Edta
Homozygous Variant In Tkfc Abolishing Triokinase Activities Is Associated With Isolated Immunodeficiency
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase / Phosphodiesterase Enpp3 Elicited By Edta
Alternative Splicing Of The Last Tkfc Intron Yields Transcripts Differentially Expressed In Human Tissues That Code In Vitro For A Protein Devoid Of Triokinase And Fmn Cyclase Activity
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase / Phosphodiesterase Enpp3 Elicited By Edta
Alternative Splicing Of The Last Tkfc Intron Yields Transcripts Differentially Expressed In Human Tissues That Code In Vitro For A Protein Devoid Of Triokinase And Fmn Cyclase Activity
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Enpp3 Elicited By Edta
Alternative Splicing Of The Last Tkfc Intron Yields Transcripts Differentially Expressed In Human Tissues That Code In Vitro For A Protein Devoid Of Triokinase And Fmn Cyclase Activity
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Enpp3 Elicited By Edta
Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Enpp3 Elicited By Edta
Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes
Genomic Distribution Of Pro-Virulent Cpdb-Like Genes In Eubacteria And Comparison Of The Enzyme Specificity Of Cpdb-Like Proteins From Salmonella Enterica, Escherichia Coli And Streptococcus Suis
Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes
Genomic Distribution Of Pro-Virulent Cpdb-Like Genes In Eubacteria And Comparison Of The Enzyme Specificity Of Cpdb-Like Proteins From Salmonella Enterica, Escherichia Coli And Streptococcus Suis
The Tkfc Ala185thr Variant, Reported As ‘null’ For Fructose Metabolism, Is Fully Active As Triokinase
Genomic Distribution Of Pro-Virulent Cpdb-Like Genes In Eubacteria And Comparison Of The Enzyme Specificity Of Cpdb-Like Proteins From Salmonella Enterica, Escherichia Coli And Streptococcus Suis
The Tkfc Ala185thr Variant, Reported As ‘null’ For Fructose Metabolism, Is Fully Active As Triokinase
Enzyme Characterization Of Pro-Virulent Snta, A Cell Wall-Anchored Protein Of Streptococcus Suis, With Phosphodiesterase Activity On Cyclic-Di-Amp At A Level Suited To Limit The Innate Immune System
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Enzyme Characterization Of Pro-Virulent Snta, A Cell Wall-Anchored Protein Of Streptococcus Suis, With Phosphodiesterase Activity On Cyclic-Di-Amp At A Level Suited To Limit The Innate Immune System
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Enzyme Characterization Of Pro-Virulent Snta, A Cell Wall-Anchored Protein Of Streptococcus Suis, With Phosphodiesterase Activity On Cyclic-Di-Amp At A Level Suited To Limit The Innate Immune System
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Substrate Specificity Of Chimeric Enzymes Formed By Interchange Of The Catalytic And Specificity Domains Of The 5′-Nucleotidase Usha And The 3′-Nucleotidase Cpdb
Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations*
Substrate Specificity Of Chimeric Enzymes Formed By Interchange Of The Catalytic And Specificity Domains Of The 5′-Nucleotidase Usha And The 3′-Nucleotidase Cpdb
Article Molecular Dissection Of Escherichia Coli Cpdb: Roles Of The N Domain In Catalysis And Phosphate Inhibition, And Of The C Domain In Substrate Specificity And Adenosine Inhibition
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Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations
Article Molecular Dissection Of Escherichia Coli Cpdb: Roles Of The N Domain In Catalysis And Phosphate Inhibition, And Of The C Domain In Substrate Specificity And Adenosine Inhibition
Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations
Closure Of The Human Tkfc Active Site: Comparison Of The Apoenzyme And The Complexes Formed With Either Triokinase Or Fmn Cyclase Substrates
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Closure Of The Human Tkfc Active Site: Comparison Of The Apoenzyme And The Complexes Formed With Either Triokinase Or Fmn Cyclase Substrates
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Identification Of Human And Rat Fad-Amp Lyase (Cyclic Fmn Forming) As Atp-Dependent Dihydroxyacetone Kinases
Fluorimetric Hplc Detection Of Endogenous Riboflavin 4′,5′- Cyclic Phosphate In Rat Liver At Nanomolar Concentrations
Identification Of Human And Rat Fad-Amp Lyase (Cyclic Fmn Forming) As Atp-Dependent Dihydroxyacetone Kinases
Fluorimetric Hplc Detection Of Endogenous Riboflavin 4′,5′- Cyclic Phosphate In Rat Liver At Nanomolar Concentrations
Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase
Fluorimetric Hplc Detection Of Endogenous Riboflavin 4′,5′- Cyclic Phosphate In Rat Liver At Nanomolar Concentrations
Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase
Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function
Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase
Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function
Purification, Characterization, And Substrate And Inhibitor Structure-Activity Studies Of Rat Liver Fad-Amp Lyase (Cyclizing): Preference For Fad And Specificity For Splitting Ribonucleoside Diphosphate-X Into Ribonucleotide And A Five-Atom Cyclic Phosphodiester Of X, Either A Monocyclic Compound Or A Cis-Bicyclic Phosphodiester-Pyranose Fusion
Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function
Purification, Characterization, And Substrate And Inhibitor Structure-Activity Studies Of Rat Liver Fad-Amp Lyase (Cyclizing): Preference For Fad And Specificity For Splitting Ribonucleoside Diphosphate-X Into Ribonucleotide And A Five-Atom Cyclic Phosphodiester Of X, Either A Monocyclic Compound Or A Cis-Bicyclic Phosphodiester-Pyranose Fusion
Inhibition And Activation Of Enzymes. The Effect Of A Modifier On The Reaction Rate And On Kinetic Parameters
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Inhibition And Activation Of Enzymes. The Effect Of A Modifier On The Reaction Rate And On Kinetic Parameters
An Easy Procedure To Transform The Ratio Of Two Polynomials Of First Degree Into Michaelis-Menten-Type Equations. Application To The Ordered Uni Bi Enzyme Mechanism
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An Easy Procedure To Transform The Ratio Of Two Polynomials Of First Degree Into Michaelis-Menten-Type Equations. Application To The Ordered Uni Bi Enzyme Mechanism
Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase.
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Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase.
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Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase.
The Simulated Purification Of An Enzyme As A 'dry' Practical Within An Introductory Course Of Biochemistry
Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase
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Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase
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Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol
Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol
Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol
Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol
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Detection Of Specific Glucose-3-Phosphatase Activity In Rat Liver
Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose
Detection Of Specific Glucose-3-Phosphatase Activity In Rat Liver
Rat Liver Mitochondrial Adp-Ribose Pyrophosphatase In The Matrix Space With Low K(M) For Free Adp-Ribose
Detection Of Specific Glucose-3-Phosphatase Activity In Rat Liver
Rat Liver Mitochondrial Adp-Ribose Pyrophosphatase In The Matrix Space With Low K(M) For Free Adp-Ribose
Enzyme Inhibition As Visualized With The Reservoir Model: Relationships Between I50 And Inhibition Constant(S) Of An Enzyme Inhibitor
Rat Liver Mitochondrial Adp-Ribose Pyrophosphatase In The Matrix Space With Low K(M) For Free Adp-Ribose
Enzyme Inhibition As Visualized With The Reservoir Model: Relationships Between I50 And Inhibition Constant(S) Of An Enzyme Inhibitor
A Tridimensional Representation Of Enzyme Inhibition Useful For Diagnostic Purposes
Enzyme Inhibition As Visualized With The Reservoir Model: Relationships Between I50 And Inhibition Constant(S) Of An Enzyme Inhibitor
A Tridimensional Representation Of Enzyme Inhibition Useful For Diagnostic Purposes
Apoptosis And Disease
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Alcohol Esterification Reactions And Mechanisms Of Snake Venom 5′‐nucleotide Phosphodiesterase
Enzyme Saturation And Inhibition Kinetics Studied From Multiple Progress Curves Recorded Spectrophotometrically From Single Reaction Mixtures For Adp-Ribose Pyrophosphatase
A Program To Calculate The Isoelectric Point Of Macromolecules
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Methanol Esterification Reactions Catalyzed By Snake Venom And Bovine Intestinal 5′‐nucleotide Phosphodiesterases: Formation Of Nucleoside 5′‐monophosphate Methyl Esters From Guanosine 5′‐triphosphate And Other Nucleoside 5′‐polyphosphates
Particulate Diadenosine 5′,5‴-P1,p3-Triphosphate Hydrolases In Rat Brain: Two Specific Dinucleoside Triphosphatases And Two Phosphodiesterase I-Like Hydrolases
Methanol Esterification Reactions Catalyzed By Snake Venom And Bovine Intestinal 5′‐nucleotide Phosphodiesterases: Formation Of Nucleoside 5′‐monophosphate Methyl Esters From Guanosine 5′‐triphosphate And Other Nucleoside 5′‐polyphosphates
Particulate Diadenosine 5′,5‴-P1,p3-Triphosphate Hydrolases In Rat Brain: Two Specific Dinucleoside Triphosphatases And Two Phosphodiesterase I-Like Hydrolases
Purification To Homogeneity Of Rat Liver Dinucleoside Tetraphosphatase By Affinity Elution With Adenosine 5′-Tetraphosphate
Particulate Diadenosine 5′,5‴-P1,p3-Triphosphate Hydrolases In Rat Brain: Two Specific Dinucleoside Triphosphatases And Two Phosphodiesterase I-Like Hydrolases
Purification To Homogeneity Of Rat Liver Dinucleoside Tetraphosphatase By Affinity Elution With Adenosine 5′-Tetraphosphate
Theoretical Isoelectric Points And Electric Charges Of Mutated Human Hemoglobin Subunits
Purification To Homogeneity Of Rat Liver Dinucleoside Tetraphosphatase By Affinity Elution With Adenosine 5′-Tetraphosphate
Theoretical Isoelectric Points And Electric Charges Of Mutated Human Hemoglobin Subunits
A Low Km Nucleoside 3′(2′),5′-Biphosphate 3′(2′)-Phosphophydrolase From Rat Liver
Theoretical Isoelectric Points And Electric Charges Of Mutated Human Hemoglobin Subunits
A Low Km Nucleoside 3′(2′),5′-Biphosphate 3′(2′)-Phosphophydrolase From Rat Liver
Computer Program For The Reservoir Model Of Metabolic Crossroads
A Low Km Nucleoside 3′(2′),5′-Biphosphate 3′(2′)-Phosphophydrolase From Rat Liver
Computer Program For The Reservoir Model Of Metabolic Crossroads
An Algorithm For The Computer Calculation Of The Coefficients Of A Polynomial That Allows Determination Of Isoelectric Points Of Proteins And Other Macromolecules
Computer Program For The Reservoir Model Of Metabolic Crossroads
An Algorithm For The Computer Calculation Of The Coefficients Of A Polynomial That Allows Determination Of Isoelectric Points Of Proteins And Other Macromolecules
A Specific, Low Km Adp-Ribose Pyrophosphatase From Rat Liver
An Algorithm For The Computer Calculation Of The Coefficients Of A Polynomial That Allows Determination Of Isoelectric Points Of Proteins And Other Macromolecules
A Specific, Low Km Adp-Ribose Pyrophosphatase From Rat Liver
Phosphoglycerate Kinase From Yeast Synthesizes Guanosine 5'-Tetraphosphate
A Specific, Low Km Adp-Ribose Pyrophosphatase From Rat Liver
Phosphoglycerate Kinase From Yeast Synthesizes Guanosine 5'-Tetraphosphate
Hydrolysis Of Bis(5'-Nucleosidyl) Polyphosphates By Escherichia Coli 5'-Nucleotidase
Phosphoglycerate Kinase From Yeast Synthesizes Guanosine 5'-Tetraphosphate
Hydrolysis Of Bis(5'-Nucleosidyl) Polyphosphates By Escherichia Coli 5'-Nucleotidase
Isoelectric Points Of Proteins: Theoretical Determination
Hydrolysis Of Bis(5'-Nucleosidyl) Polyphosphates By Escherichia Coli 5'-Nucleotidase
Isoelectric Points Of Proteins: Theoretical Determination
Characterization Of The Interferon- And Virus-Inducible Mx Promoter
Isoelectric Points Of Proteins: Theoretical Determination
Characterization Of The Interferon- And Virus-Inducible Mx Promoter
Organization Of The Murine Mx Gene And Characterization Of Its Interferon- And Virus-Inducible Promoter
Characterization Of The Interferon- And Virus-Inducible Mx Promoter
Organization Of The Murine Mx Gene And Characterization Of Its Interferon- And Virus-Inducible Promoter
The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)
Organization Of The Murine Mx Gene And Characterization Of Its Interferon- And Virus-Inducible Promoter
The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)
Binding Of Zinc(Ii) To Β-D-Fructose 2,6-Bisphosphate
The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)
Binding Of Zinc(Ii) To Β-D-Fructose 2,6-Bisphosphate
Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides
Binding Of Zinc(Ii) To Β-D-Fructose 2,6-Bisphosphate
Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides
Mitochondrial Location Of Rat Liver Dinucleoside Triphosphatase
Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides
Mitochondrial Location Of Rat Liver Dinucleoside Triphosphatase
Occurrence Of Dinucleosidetriphosphatase In The Cytosol And Particulate Fractions From Rat Liver
Mitochondrial Location Of Rat Liver Dinucleoside Triphosphatase
Occurrence Of Dinucleosidetriphosphatase In The Cytosol And Particulate Fractions From Rat Liver
Dinucleosidetriphosphatase From Rat Brain
Occurrence Of Dinucleosidetriphosphatase In The Cytosol And Particulate Fractions From Rat Liver
Dinucleosidetriphosphatase From Rat Brain
Diadenosine Tetraphosphate Activates Amp Deaminase From Rat Muscle
Dinucleosidetriphosphatase From Rat Brain
Diadenosine Tetraphosphate Activates Amp Deaminase From Rat Muscle
Two Low K(M) Hydrolytic Activities On Dinucleoside 5',5'''-P1,p4-Tetraphosphates In Rat Liver. Characterization As The Specific Dinucleoside Tetraphosphatase And A Phosphodiesterase I-Like Enzyme
Diadenosine Tetraphosphate Activates Amp Deaminase From Rat Muscle
Two Low K(M) Hydrolytic Activities On Dinucleoside 5',5'''-P1,p4-Tetraphosphates In Rat Liver. Characterization As The Specific Dinucleoside Tetraphosphatase And A Phosphodiesterase I-Like Enzyme
Presence Of Cytidine 5′-Tetraphosphate In Commercial Samples Of Cytidine 5′-Triphosphate
Two Low K(M) Hydrolytic Activities On Dinucleoside 5',5'''-P1,p4-Tetraphosphates In Rat Liver. Characterization As The Specific Dinucleoside Tetraphosphatase And A Phosphodiesterase I-Like Enzyme
Presence Of Cytidine 5′-Tetraphosphate In Commercial Samples Of Cytidine 5′-Triphosphate
Dinucleosidetetraphosphatase Inhibition By Zn(Ii)
Presence Of Cytidine 5′-Tetraphosphate In Commercial Samples Of Cytidine 5′-Triphosphate
Dinucleosidetetraphosphatase Inhibition By Zn(Ii)
A Cut-Out Model Of The Α-Helix For Student Use
Dinucleosidetetraphosphatase Inhibition By Zn(Ii)
A Cut-Out Model Of The Α-Helix For Student Use
Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.
A Cut-Out Model Of The Α-Helix For Student Use
Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.
Distribución Y Propiedades De La Dinucleosidotetrafosfatosa En Diversos Tejidos De Rata
Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.
Distribución Y Propiedades De La Dinucleosidotetrafosfatosa En Diversos Tejidos De Rata
The Regulation Of Glycolysis In The Hepatopancreas Of The Sea Mussel Mytilus Edulis L.
Distribución Y Propiedades De La Dinucleosidotetrafosfatosa En Diversos Tejidos De Rata
The Regulation Of Glycolysis In The Hepatopancreas Of The Sea Mussel Mytilus Edulis L.
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Enpp3 Elicited By Edta: Free Amino Acids Accelerate The Time-Dependent Inactivation..: A. Romero Et Al.
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