A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase

被引:20
作者
Bertoldi, M
Cellini, B
Maras, B
Voltattorni, CB [1 ]
机构
[1] Univ Verona, Dipartimento Sci Neurol & Vis, Sez Chima Biol, I-37100 Verona, Italy
[2] Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy
来源
FEBS LETTERS | 2005年 / 579卷 / 23期
关键词
Dopa decarboxylase; pyridoxal 5'-phosphate; catalytic quinonoid; methyl ester; oxidative deamination;
D O I
10.1016/j.febslet.2005.08.029
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:5175 / 5180
页数:6
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