| EC |
1.3.1.78 |
| Accepted name: |
arogenate dehydrogenase (NADP+) |
| Reaction: |
L-arogenate + NADP+ = L-tyrosine + NADPH + CO2 |
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For diagram of phenylalanine and tyrosine biosynthesis, click here |
| Glossary: |
L-arogenate = 1-[(2S)-2-amino-2-carboxyethyl]-4-hydroxycyclohexa-2,5-diene-1-carboxylate |
| Other name(s): |
arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa |
| Systematic name: |
L-arogenate:NADP+ oxidoreductase (decarboxylating) |
| Comments: |
Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NADP+-dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly [2,3]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 64295-75-6 |
| References: |
| 1. |
Gaines, C.G., Byng, G.S., Whitaker, R.J. and Jensen, R.A. L-Tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes. Planta 156 (1982) 233–240. [PMID: 24272471] |
| 2. |
Rippert, P. and Matringe, M. Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana. Eur. J. Biochem. 269 (2002) 4753–4761. [DOI] [PMID: 12354106] |
| 3. |
Bonner, C.A., Jensen, R.A., Gander, J.E. and Keyhani, N.O. A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. Biochem. J. 382 (2004) 279–291. [DOI] [PMID: 15171683] |
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| [EC 1.3.1.78 created 2005] |
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