The reactions of Dopa decarboxylase (DDC) with Land D-enantiomers of tryptophan methyl ester are described. Although both the enantiomers bind to the active site of the enzyme with similar affinity, their binding modes are different. L-enantiomer binds in an unproductive mode, while D-enantiomer acts as an oxidative deamination substrate. For the first time a quinonoid has been detected as intermediate of this reaction. By using rapid-scanning stopped-flow kinetic technique rate constants for formation and decay of this species have been determined. All these data, besides validating the functional DDC active site model, represent an important step toward the elucidation of the catalytic pathway of oxidative deamination. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase / Mariarita, Bertoldi; Barbara, Cellini; Maras, Bruno; Carla Borri, Voltattorni. - In: FEBS LETTERS. - ISSN 0014-5793. - 579:23(2005), pp. 5175-5180. [10.1016/j.febslet.2005.08.029]
A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase
MARAS, Bruno;
2005
Abstract
The reactions of Dopa decarboxylase (DDC) with Land D-enantiomers of tryptophan methyl ester are described. Although both the enantiomers bind to the active site of the enzyme with similar affinity, their binding modes are different. L-enantiomer binds in an unproductive mode, while D-enantiomer acts as an oxidative deamination substrate. For the first time a quinonoid has been detected as intermediate of this reaction. By using rapid-scanning stopped-flow kinetic technique rate constants for formation and decay of this species have been determined. All these data, besides validating the functional DDC active site model, represent an important step toward the elucidation of the catalytic pathway of oxidative deamination. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
