EC |
1.3.1.43 |
Accepted name: |
arogenate dehydrogenase |
Reaction: |
L-arogenate + NAD+ = L-tyrosine + NADH + 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); cyclohexadienyl dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); L-arogenate:NAD+ oxidoreductase; arogenate dehydrogenase (NAD+) |
Systematic name: |
L-arogenate:NAD+ 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). NAD+-specific enzymes have been reported from some bacteria [2] and plants [3]. Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 64295-75-6 |
References: |
1. |
Stenmark, S.L., Pierson, D.L., Jensen, R.A. and Glover, G.I. Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway. Nature 247 (1974) 290–292. [PMID: 4206476] |
2. |
Byng, G.S., Whitaker, R.J., Gherna, R.L. and Jensen, R.A. Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae. J. Bacteriol. 144 (1980) 247–257. [PMID: 7419490] |
3. |
Byng, G., Whitaker, R., Flick, C. and Jensen, R.A. Enzymology of L-tyrosine biosynthesis in corn (Zea mays). Phytochemistry 20 (1981) 1289–1292. |
4. |
Mayer, E., Waldner-Sander, S., Keller, B., Keller, E. and Lingens, F. Purification of arogenate dehydrogenase from Phenylobacterium immobile. FEBS Lett. 179 (1985) 208–212. [DOI] [PMID: 3967752] |
5. |
Lingens, F., Keller, E. and Keller, B. Arogenate dehydrogenase from Phenylobacterium immobile. Methods Enzymol. 142 (1987) 513–518. [DOI] |
6. |
Zamir, L.O., Tiberio, R., Devor, K.A., Sauriol, F., Ahmad, S. and Jensen, R.A. Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa. J. Biol. Chem. 263 (1988) 17284–17290. [PMID: 2972718] |
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[EC 1.3.1.43 created 1989, modified 2003, modified 2005, modified 2015] |
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EC |
1.3.1.78 |
Accepted name: |
arogenate dehydrogenase (NADP+) |
Reaction: |
L-arogenate + NADP+ = L-tyrosine + NADPH + CO2 |
|
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, 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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EC |
1.3.1.79 |
Accepted name: |
arogenate dehydrogenase [NAD(P)+] |
Reaction: |
L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + 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); cyclohexadienyl dehydrogenase; pretyrosine dehydrogenase (ambiguous) |
Systematic name: |
L-arogenate:NAD(P)+ 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). Enzymes that can utilize both cofactors have been reported from some Proteobacteria, including Burkholderia caryophylli, Burkholderia cepacia, Pseudomonas marginata and Delftia acidovorans. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64295-75-6 |
References: |
1. |
Byng, G.S., Whitaker, R.J., Gherna, R.L. and Jensen, R.A. Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae. J. Bacteriol. 144 (1980) 247–257. [PMID: 7419490] |
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[EC 1.3.1.79 created 2005] |
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EC |
2.6.1.78 |
Accepted name: |
aspartate—prephenate aminotransferase |
Reaction: |
L-arogenate + oxaloacetate = prephenate + L-aspartate |
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For diagram of phenylalanine and tyrosine biosynthesis, click here |
Other name(s): |
prephenate transaminase (ambiguous); PAT (ambiguous); prephenate aspartate aminotransferase; L-aspartate:prephenate aminotransferase |
Systematic name: |
L-arogenate:oxaloacetate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate—prephenate aminotransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
De-Eknamkul, W. and Ellis, B.E. Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures. Arch. Biochem. Biophys. 267 (1988) 87–94. [DOI] [PMID: 3196038] |
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[EC 2.6.1.78 created 2005] |
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EC |
2.6.1.79 |
Accepted name: |
glutamate—prephenate aminotransferase |
Reaction: |
L-arogenate + 2-oxoglutarate = prephenate + L-glutamate |
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For diagram of phenylalanine and tyrosine biosynthesis, click here |
Other name(s): |
prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase |
Systematic name: |
L-arogenate:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate—prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bonner, C.A. and Jensen, R.A. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 238 (1985) 237–246. [DOI] [PMID: 3985619] |
2. |
Siehl, D.L., Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase. Z. Naturforsch. 41 (1986) 79–86. [PMID: 2939644] |
3. |
Bonner, C. and Jensen, R. Prephenate aminotransferase. Methods Enzymol. 142 (1987) 479–487. [PMID: 3298985] |
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[EC 2.6.1.79 created 2005] |
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EC |
4.2.1.91 |
Accepted name: |
arogenate dehydratase |
Reaction: |
L-arogenate = L-phenylalanine + H2O + CO2 |
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For diagram of phenylalanine and tyrosine biosynthesis, click here |
Other name(s): |
carboxycyclohexadienyl dehydratase; L-arogenate hydro-lyase (decarboxylating) |
Systematic name: |
L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming) |
Comments: |
Also acts on prephenate and D-prephenyllactate. cf. EC 4.2.1.51, prephenate dehydratase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76600-70-9 |
References: |
1. |
Fischer, R. and Jensen, R. Arogenate dehydratase. Methods Enzymol. 142 (1987) 495–502. [PMID: 3600377] |
2. |
Zamir, L.O., Tiberio, R., Devor, K.A., Sauriol, F., Ahmad, S. and Jensen, R.A. Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa. J. Biol. Chem. 263 (1988) 17284–17290. [PMID: 2972718] |
3. |
Siehl, D.L. and Conn, E.E. Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 260 (1988) 822–829. [DOI] [PMID: 3124763] |
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[EC 4.2.1.91 created 1992, modified 2005] |
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