Reversing the Substrate Specificities of Phenylalanine and Tyrosine Hydroxylase:  Aspartate 425 of Tyrosine Hydroxylase Is Essential forl-DOPA Formation†

Biochemistry ◽  
2000 ◽  
Vol 39 (32) ◽  
pp. 9652-9661 ◽  
Author(s):  
S. Colette Daubner ◽  
Julie Melendez ◽  
Paul F. Fitzpatrick
1990 ◽  
Vol 268 (2) ◽  
pp. 525-528 ◽  
Author(s):  
M H Fukami ◽  
J Haavik ◽  
T Flatmark

Incubation of bovine chromaffin cells with L-[14C]phenylalanine resulted in label accumulation in catecholamines at about 30% of the rate seen with L-tyrosine as precursor. Studies with purified tyrosine hydroxylase (EC 1.14.16.2) showed that the enzyme catalysed the hydroxylation of L-phenylalanine first to L-p-tyrosine and then to 3,4-dihydroxyphenylalanine (DOPA). No evidence for a significant involvement of an L-m-tyrosine intermediate in DOPA formation was found.


1990 ◽  
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pp. 625-632 ◽  
Author(s):  
Akira Ishii ◽  
Masako Hagihara ◽  
Sadao Matsuura ◽  
Kohichi Uchida ◽  
Kazutoshi Kiuchi ◽  
...  

2001 ◽  
Vol 13 (1) ◽  
pp. 57-67 ◽  
Author(s):  
Tomas Gonzalez-Hernandez ◽  
Pedro Barroso-Chinea ◽  
Abraham Acevedo ◽  
Eduardo Salido ◽  
Manuel Rodriguez
Keyword(s):  

2018 ◽  
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Ryan W. Logan ◽  
Puja K. Parekh ◽  
Wilbur Williams III ◽  
Gabrielle Kaplan ◽  
Darius Becker-Krail ◽  
...  

2014 ◽  
Vol 13 (5) ◽  
pp. 896-908 ◽  
Author(s):  
Mattia Vicario ◽  
Adriana Zagari ◽  
Vincenzo Granata ◽  
Francesca Munari ◽  
Stefano Mammi ◽  
...  

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