cyclohexadieny/prephenate dehydrogenase [EC:1.3.1.43 1.3.1.12]

PMID:7916685

Zhao G, Xia T, Ingram LO, Jensen RA

An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis.

Eur J Biochem 212:157-65 (1993)
DOI:10.1111/j.1432-1033.1993.tb17646.x

arogenate dehydrogenase (NADP+) [EC:1.3.1.78]

PMID:15171683

Bonner CA, Jensen RA, Gander JE, Keyhani NO

A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from  Synechocystis.

Biochem J 382:279-91 (2004)
DOI:10.1042/BJ20031809

[syn:slr2081]

arogenate dehydrogenase (NADP+), plant [EC:1.3.1.78]

PMID:12354106

Rippert P, Matringe M

Purification and kinetic analysis of the two recombinant arogenate dehydrogenase  isoforms of Arabidopsis thaliana.

Eur J Biochem 269:4753-61 (2002)
DOI:10.1046/j.1432-1033.2002.03172.x

[ath:AT5G34930 AT1G15710]

PMID:19136569

Rippert P, Puyaubert J, Grisollet D, Derrier L, Matringe M

Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis.

Plant Physiol 149:1251-60 (2009)
DOI:10.1104/pp.108.130070

Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor

L-arogenate:NAD+ oxidoreductase (decarboxylating)

L-arogenate + NAD+ = L-tyrosine + NADH + CO2 [RN:R00732]

R00732

L-arogenate [CPD:C00826];
NAD+ [CPD:C00003]

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.

EC 1.3.1.43 created 1989, modified 2003, modified 2005, modified 2015

1  [PMID:4206476]

Stenmark SL, Pierson DL, Jensen RA, Glover GI.

Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway.

Nature. 247 (1974) 290-2.

2  [PMID:7419490]

Byng GS, Whitaker RJ, Gherna RL, Jensen RA

Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae.

J. Bacteriol. 144 (1980) 247-57.

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  [PMID:3967752]

Mayer E, Waldner-Sander S, Keller B, Keller E, Lingens F.

Purification of arogenate dehydrogenase from Phenylobacterium immobile.

FEBS. Lett. 179 (1985) 208-12.

5

Lingens, F., Keller, E. and Keller, B.

Arogenate dehydrogenase from Phenylobacterium immobile.

Methods Enzymol. 142 (1987) 513-518.

6  [PMID:2972718]

Zamir LO, Tiberio R, Devor KA, Sauriol F, Ahmad S, Jensen RA.

Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa.

J. Biol. Chem. 263 (1988) 17284-90.

Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor

L-arogenate:NADP+ oxidoreductase (decarboxylating)

L-arogenate + NADP+ = L-tyrosine + NADPH + CO2 [RN:R00733]

R00733

L-arogenate [CPD:C00826];
NADP+ [CPD:C00006]

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].

EC 1.3.1.78 created 2005