3 results on '"Gilabert, M. Ángeles"'
Search Results
2. Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase
- Author
-
Espín de Gea, Juan Carlos, Varón, Ramón, Fenoll, Lorena G., Gilabert, M. Ángeles, García-Ruíz, Pedro, Tudela, José, García-Cánovas, Francisco, Comisión Interministerial de Ciencia y Tecnología, CICYT (España), and Ministerio de Educación y Ciencia (España)
- Subjects
Mushroom ,Enzyme kinetics ,Monophenolase ,Diphenolase ,3-methyl-2-benzothiazolinone hydrazone (MBTH) - Abstract
10 pages, 1 figure, 5 tables.-- Online version published Apr. 2002., This paper reports a quantitative study of the effect of ring substituents in the 1-position of the aromatic ring on the rate of monophenol hydroxylation and o-diphenol oxidation catalyzed by tyrosinase. A possible correlation between the electron density of the carbon atom supporting the oxygen from the monophenolic hydroxyl group and the V Mmax values for each monophenol was found. In the case of o-diphenols the same effect was observed but the size of the side-chain became very important. NMR studies on the monophenols justified the sequence of the V Mmax values obtained. As regards the o-diphenols, on the other hand, only a fair correlation between NMR and V Dmax values was observed due to the effect of the molecular size of the ring substituent. From these data, it can be concluded that the redox step (k33) is not the rate-determining step of the reaction mechanism. Thus, the monophenols are converted into diphenols, but the order of specificities towards monophenols is different to that of o-diphenols. The rate-limiting step of the monophenolase activity could be the nucleophilic attack (k51) of the oxygen atom of the hydroxyl group on the copper atoms of the active site of the enzyme. This step could also be similar to or have a lower rate of attack than the electrophilic attack (k52) of the oxygen atom of the active site of oxytyrosinase on the C-3 of the monophenolic ring. However, the rate-limiting step in the diphenolase activity of tyrosinase could be related to both the nucleophilic power of the oxygen atom belonging to the hydroxyl group at the carbon atom in the 3-position (k32) and to the size of the substituent side-chain. On the basis of the results obtained, kinetic and structural models describing the monophenolase and diphenolase reaction mechanisms for tyrosinase are proposed., This paper was partially supported by the `Comisión Interministerial de Ciencia y Tecnología', project number CICYT PB98-0403-CO2. J. C. E. has a fellowship from the Programa Nacional de Formación del Personal Investigador, Ministerio de Educación y Ciencia (Spain), reference AP93 34785457.
- Published
- 2000
3. Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase
- Author
-
Comisión Interministerial de Ciencia y Tecnología, CICYT (España), Ministerio de Educación y Ciencia (España), Espín de Gea, Juan Carlos, Varón, Ramón, Fenoll, Lorena G., Gilabert, M. Ángeles, García-Ruíz, Pedro, Tudela, José, García-Cánovas, Francisco, Comisión Interministerial de Ciencia y Tecnología, CICYT (España), Ministerio de Educación y Ciencia (España), Espín de Gea, Juan Carlos, Varón, Ramón, Fenoll, Lorena G., Gilabert, M. Ángeles, García-Ruíz, Pedro, Tudela, José, and García-Cánovas, Francisco
- Abstract
This paper reports a quantitative study of the effect of ring substituents in the 1-position of the aromatic ring on the rate of monophenol hydroxylation and o-diphenol oxidation catalyzed by tyrosinase. A possible correlation between the electron density of the carbon atom supporting the oxygen from the monophenolic hydroxyl group and the V Mmax values for each monophenol was found. In the case of o-diphenols the same effect was observed but the size of the side-chain became very important. NMR studies on the monophenols justified the sequence of the V Mmax values obtained. As regards the o-diphenols, on the other hand, only a fair correlation between NMR and V Dmax values was observed due to the effect of the molecular size of the ring substituent. From these data, it can be concluded that the redox step (k33) is not the rate-determining step of the reaction mechanism. Thus, the monophenols are converted into diphenols, but the order of specificities towards monophenols is different to that of o-diphenols. The rate-limiting step of the monophenolase activity could be the nucleophilic attack (k51) of the oxygen atom of the hydroxyl group on the copper atoms of the active site of the enzyme. This step could also be similar to or have a lower rate of attack than the electrophilic attack (k52) of the oxygen atom of the active site of oxytyrosinase on the C-3 of the monophenolic ring. However, the rate-limiting step in the diphenolase activity of tyrosinase could be related to both the nucleophilic power of the oxygen atom belonging to the hydroxyl group at the carbon atom in the 3-position (k32) and to the size of the substituent side-chain. On the basis of the results obtained, kinetic and structural models describing the monophenolase and diphenolase reaction mechanisms for tyrosinase are proposed.
- Published
- 2000
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