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1
Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism
Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism
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Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism

Torre, Fernando de la ; Santis, Laura De ; Suárez, María Fernanda ; Crespillo, Remedios ; Cánovas, Francisco M

The Plant journal : for cell and molecular biology, 2006-05, Vol.46 (3), p.414-425 [Periódico revisado por pares]

Oxford, UK: Oxford, UK : Blackwell Publishing Ltd

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2
Molecular Modeling and Site-Directed Mutagenesis Reveal Essential Residues for Catalysis in a Prokaryote-Type Aspartate Aminotransferase
Molecular Modeling and Site-Directed Mutagenesis Reveal Essential Residues for Catalysis in a Prokaryote-Type Aspartate Aminotransferase
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Molecular Modeling and Site-Directed Mutagenesis Reveal Essential Residues for Catalysis in a Prokaryote-Type Aspartate Aminotransferase

de la Torre, Fernando ; Moya-García, Aurelio A ; Suárez, María-Fernanda ; Rodríguez-Caso, Carlos ; Cañas, Rafael A ; Sánchez-Jiménez, Francisca ; Cánovas, Francisco M

Plant physiology (Bethesda), 2009-04, Vol.149 (4), p.1648-1660 [Periódico revisado por pares]

Rockville, MD: American Society of Plant Biologists

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3
Changes in NADP + -linked isocitrate dehydrogenase during tomato fruit ripening: Characterization of the predominant cytosolic enzyme from green and ripe pericarp
Changes in NADP + -linked isocitrate dehydrogenase during tomato fruit ripening: Characterization of the predominant cytosolic enzyme from green and ripe pericarp
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Changes in NADP + -linked isocitrate dehydrogenase during tomato fruit ripening: Characterization of the predominant cytosolic enzyme from green and ripe pericarp

Gallardo, Fernando ; Gálvez, Susana ; Gadal, Pierre ; Cánovas, Francisco M.

Planta, 1995-03, Vol.196 (1), p.148-154 [Periódico revisado por pares]

Berlin: Springer-Verlag

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4
Antifolate Activity of Epigallocatechin Gallate against Stenotrophomonas maltophilia
Antifolate Activity of Epigallocatechin Gallate against Stenotrophomonas maltophilia
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Antifolate Activity of Epigallocatechin Gallate against Stenotrophomonas maltophilia

María Dolores Navarro-Martínez ; Enma Navarro-Perán ; Juan Cabezas-Herrera ; Joaquín Ruiz-Gómez ; Francisco García-Cánovas ; José Neptuno Rodríguez-López

Antimicrobial Agents and Chemotherapy, 2005-07, Vol.49 (7), p.2914-2920 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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5
Production of o-diphenols by immobilized mushroom tyrosinase
Production of o-diphenols by immobilized mushroom tyrosinase
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Production of o-diphenols by immobilized mushroom tyrosinase

Marín-Zamora, María Elisa ; Rojas-Melgarejo, Francisco ; García-Cánovas, Francisco ; García-Ruiz, Pedro Antonio

Journal of biotechnology, 2009-01, Vol.139 (2), p.163-168 [Periódico revisado por pares]

Amsterdam: Elsevier B.V

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6
Effects of the immobilization supports on the catalytic properties of immobilized mushroom tyrosinase: A comparative study using several substrates
Effects of the immobilization supports on the catalytic properties of immobilized mushroom tyrosinase: A comparative study using several substrates
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Effects of the immobilization supports on the catalytic properties of immobilized mushroom tyrosinase: A comparative study using several substrates

Marín-Zamora, María Elisa ; Rojas-Melgarejo, Francisco ; García-Cánovas, Francisco ; García-Ruiz, Pedro Antonio

Journal of biotechnology, 2007-09, Vol.131 (4), p.388-396 [Periódico revisado por pares]

Lausanne: Elsevier B.V

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7
Stereospecificity of Mushroom Tyrosinase Immobilized on a Chiral and a Nonchiral Support
Stereospecificity of Mushroom Tyrosinase Immobilized on a Chiral and a Nonchiral Support
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Stereospecificity of Mushroom Tyrosinase Immobilized on a Chiral and a Nonchiral Support

Marín-Zamora, María Elisa ; Rojas-Melgarejo, Francisco ; García-Cánovas, Francisco ; García-Ruiz, Pedro Antonio

Journal of agricultural and food chemistry, 2007-05, Vol.55 (11), p.4569-4575 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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8
A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C
A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C
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A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C

Hiner, Alexander N. P. ; Hernández-Ruíz, Josefa ; Arnao, Marino B. ; García-Cánovas, Francisco ; Acosta, Manuel

Biotechnology and bioengineering, 1996-06, Vol.50 (6), p.655-662 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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9
Monophenolase activity of polyphenol oxidase from Verdedoncella apple
Monophenolase activity of polyphenol oxidase from Verdedoncella apple
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Monophenolase activity of polyphenol oxidase from Verdedoncella apple

Espin, Juan Carlos ; Morales, Mercedes ; Varon, Ramon ; Tudela, Jose ; Garcia-Canovas, Francisco

Journal of agricultural and food chemistry, 1995-11, Vol.43 (11), p.2807-2812 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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10
Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions
Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions
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Purification and Kinetic Characterization of an Anionic Peroxidase from Melon (Cucumis melo L.) Cultivated under Different Salinity Conditions

Rodríguez-López, Jose Neptuno ; Espín, Juan Carlos ; del Amor, Francisco ; Tudela, José ; Martínez, Vicente ; Cerdá, Antonio ; García-Cánovas, Francisco

Journal of agricultural and food chemistry, 2000-05, Vol.48 (5), p.1537-1541 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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