The Enzyme Database

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EC 1.3.1.43     
Accepted name: arogenate dehydrogenase
Reaction: L-arogenate + NAD+ = L-tyrosine + NADH + 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); 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, 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.
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]
[EC 1.3.1.43 created 1989, modified 2003, modified 2005, modified 2015]
 
 
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]
[EC 1.3.1.78 created 2005]
 
 
EC 1.3.1.79     
Accepted name: arogenate dehydrogenase [NAD(P)+]
Reaction: L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + 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); 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]
[EC 1.3.1.79 created 2005]
 
 
EC 2.6.1.78     
Accepted name: aspartate—prephenate aminotransferase
Reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate
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
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]
[EC 2.6.1.78 created 2005]
 
 
EC 2.6.1.79     
Accepted name: glutamate—prephenate aminotransferase
Reaction: L-arogenate + 2-oxoglutarate = prephenate + L-glutamate
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
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]
[EC 2.6.1.79 created 2005]
 
 
EC 4.2.1.91     
Accepted name: arogenate dehydratase
Reaction: L-arogenate = L-phenylalanine + H2O + CO2
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, 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]
[EC 4.2.1.91 created 1992, modified 2005]
 
 


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