PUBLICACIÓN

Use of potato tuber nucleotide pyrophosphatase to synthesize adenosine 5'-monophosphate methyl ester: Evidence that the solvolytic preferences of the enzyme are regulated by pH and temperature

ACCEDER A LA PUBLICACIÓN: Scopus Orcid

Agudo, A., Ribeiro, J.M., Canales, J., Cameselle, J.C.

1998 Biotechnology and Bioengineering

CITAS

2

DOI

10.1002/(sici)1097-0290(19980705)59:1<62::aid-bit8>3.0.co;2-r

EID

2-s2.0-0032486579

ISSN

0006-3592

BIBTEX

@article{Ribeiro1998,title = {Use of potato tuber nucleotide pyrophosphatase to synthesize adenosine 5{'}-monophosphate methyl ester: Evidence that the solvolytic preferences of the enzyme are regulated by pH and temperature},journal = {Biotechnology and Bioengineering},year = {1998},volume = {59},number = {1},pages = {62-67},author = {Agudo, A. and Ribeiro, J.M. and Canales, J. and Cameselle, J.C.}}

AUTORES DE LA UEX

Juan Nuno Meireles Da Silva Gonçalves Ribeiro

OTRAS PUBLICACIONES DE INTERÉS

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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
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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
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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
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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
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Identification Of Human And Rat Fad-Amp Lyase (Cyclic Fmn Forming) As Atp-Dependent Dihydroxyacetone Kinases
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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
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Inhibition And Activation Of Enzymes. The Effect Of A Modifier On The Reaction Rate And On Kinetic Parameters
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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
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A Tridimensional Representation Of Enzyme Inhibition Useful For Diagnostic Purposes
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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
The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)
Isoelectric Points Of Proteins: Theoretical Determination
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
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
Dinucleosidetriphosphatase From Rat Brain
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.
The Regulation Of Glycolysis In The Hepatopancreas Of The Sea Mussel Mytilus Edulis L.
Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.
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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