Entry
Name
arogenate dehydrogenase;
arogenic dehydrogenase (ambiguous);
cyclohexadienyl dehydrogenase (ambiguous);
pretyrosine dehydrogenase (ambiguous);
L-arogenate:NAD+ oxidoreductase;
arogenate dehydrogenase (NAD+)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
L-arogenate:NAD+ oxidoreductase (decarboxylating)
Reaction(IUBMB)
L-arogenate + NAD+ = L-tyrosine + NADH + CO2 [RN:
R00732 ]
Reaction(KEGG)
Substrate
Product
Comment
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.
History
EC 1.3.1.43 created 1989, modified 2003, modified 2005, modified 2015
Pathway
ec00400 Phenylalanine, tyrosine and tryptophan biosynthesis
ec01110 Biosynthesis of secondary metabolites
Orthology
K00220 cyclohexadieny/prephenate dehydrogenase
K24018 cyclohexadieny/prephenate dehydrogenase / 3-phosphoshikimate 1-carboxyvinyltransferase
Genes
PPUN : PP4_40010(tyrA_aroA)
PPRC : PFLCHA0_c43820(aroA1)
PMUD : NCTC8068_01765(aroA_1)
PFW : PF1751_v1c16150(aroA)
PPUU : PputUW4_01362(aroA)
PTW : TUM18999_16600(aroA)
PTAE : NCTC10697_01565(aroA)
MSHE : MAALD49_23120(aroA)
PSYC : DABAL43B_1618(aroA)
PKY : PKHYL_22090 PKHYL_22100
MCAT : MC25239_00892(aroA)
MCUN : NCTC10297_01609(aroA)
ALCA : ASALC70_04154(aroA)
MPON : MACH16_20310(aroA_2)
PLG : NCTC10937_03983(aroA_1)
RBS : RHODOSMS8_02687(tyrA)
SMEL : SM2011_c00711(tyrC)
SFD : USDA257_c50690(tyrC)
SAME : SAMCFNEI73_Ch3031(tyrC)
AVV : RvVAT039_13760(tyrC)
AVF : RvVAR031_00790(tyrC)
REC : RHECIAT_CH0004080(tyrC)
REL : REMIM1_CH03894(tyrC)
REP : IE4803_CH04183(tyrC)
REI : IE4771_CH04125(tyrC)
RGA : RGR602_CH03730(tyrC)
RPHA : AMC79_CH04014(tyrC)
NEN : NCHU2750_33520(tyrC)
BIO : BR141012304_10729(tyrC)
VGO : GJW-30_1_00717(tyrA)
BHS : BM1374165_01676(tyrC)
BTX : BM1374166_02242(tyrC)
BEZ : NCTC12898_01572(tyrC)
MAQU : Maq22A_1p32200(tyrA)
MTUN : MTUNDRAET4_0586(tyrC)
TSV : DSM104635_02909(tyrC)
RLI : RLO149_c027460(tyrC)
PHP : PhaeoP97_02393(tyrC)
PPIC : PhaeoP14_02309(tyrC)
SINL : DSM14862_00654(tyrC)
SPSE : SULPSESMR1_02431(tyrA)
RMM : ROSMUCSMR3_01256(tyrA)
AHT : ANTHELSMS3_01141(tyrA)
THAA : CFI11_06550 CFI11_12505
LALG : LentiSH36_00258(tyrC)
LVS : LOKVESSMR4R_00454(tyrA)
SPAG : sphantq_02194(tyrC)
SFLA : SPHFLASMR4Y_02396(tyrA)
SPHS : ETR14_24205 ETR14_25105
SHUM : STHU_49340(tyrC_1) STHU_49350(tyrC_2)
SVC : STVA_01960 STVA_01970
STEL : STAQ_44560(tyrC_1) STAQ_44570(tyrC_2)
ABS : AZOBR_p1130164(tyrC)
LEPV : J4558_12690 J4558_16295
» show all
Taxonomy
Reference
Authors
Stenmark SL, Pierson DL, Jensen RA, Glover GI.
Title
Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway.
Journal
Reference
Authors
Byng GS, Whitaker RJ, Gherna RL, Jensen RA
Title
Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae.
Journal
Reference
3
Authors
Byng G, Whitaker R, Flick C, Jensen RA.
Title
Enzymology of L-tyrosine biosynthesis in corn (Zea mays).
Journal
Phytochemistry 20:1289-1292 (1981)
Reference
Authors
Mayer E, Waldner-Sander S, Keller B, Keller E, Lingens F.
Title
Purification of arogenate dehydrogenase from Phenylobacterium immobile.
Journal
Reference
5
Authors
Lingens F, Keller E, Keller B.
Title
Arogenate dehydrogenase from Phenylobacterium immobile.
Journal
Methods Enzymol 142:513-518 (1987)
Reference
Authors
Zamir LO, Tiberio R, Devor KA, Sauriol F, Ahmad S, Jensen RA.
Title
Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa.
Journal
J Biol Chem 263:17284-90 (1988)
Other DBs
ExplorEnz - The Enzyme Database: 1.3.1.43
ExPASy - ENZYME nomenclature database: 1.3.1.43
LinkDB
All DBs