KEGG   ENZYME: 1.3.1.43Help
Entry
EC 1.3.1.43                 Enzyme                                 

Name
arogenate dehydrogenase;
arogenic dehydrogenase (ambiguous);
cyclohexadienyl dehydrogenase;
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
L-arogenate [CPD:C00826];
NAD+ [CPD:C00003]
Product
L-tyrosine [CPD:C00082];
NADH [CPD:C00004];
CO2 [CPD:C00011]
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
ec00401  Novobiocin biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00220  cyclohexadieny/prephenate dehydrogenase
Genes
PSO: PSYCG_06320
PUR: AOC03_00795
PALI: A3K91_1177
PSPG: AK823_06620
PSYG: AK825_06690
PSYC: DABAL43B_1618(aroA)
PSYA: AOT82_301
ACB: A1S_2276
ABM: ABSDF1252
ABY: ABAYE1207
ABN: AB57_2630
ABB: ABBFA_001168(aroA)
ABX: ABK1_1213
ABH: M3Q_2741
ABAD: ABD1_22740(aroA)
ABAZ: P795_5535
ABAU: IX87_07480
ABAA: IX88_14375
ACC: BDGL_001767(aroA)
ACI: ACIAD2222
MCS: DR90_991(aroA)
MCAT: MC25239_00892(aroA)
MLO: mll3535
MES: Meso_3085
AMIH: CO731_01722(tyrC)
PLA: Plav_1584
SME: SMc00711(tyrC)
SMX: SM11_chr2823(tyrC)
SMI: BN406_02519(tyrC)
SMEL: SM2011_c00711(tyrC)
SMER: DU99_14760
SMD: Smed_2549
RHI: NGR_c27070(tyrC)
SFH: SFHH103_02632(tyrC)
SFD: USDA257_c50690(tyrC)
SAME: SAMCFNEI73_Ch3031(tyrC)
EAD: OV14_0123(tyrC)
ATU: Atu3611(tyrC)
ARA: Arad_4216(tyrC)
ATF: Ach5_34600(tyrC)
AVI: Avi_4033(tyrC)
RET: RHE_CH03809(tyrC)
REC: RHECIAT_CH0004080(tyrC)
REL: REMIM1_CH03894(tyrC)
REI: IE4771_CH04125(tyrC)
REP: IE4803_CH04183(tyrC)
RLE: RL4337(tyrC)
RLG: Rleg_3872
RIR: BN877_II0616(tyrC)
RHL: LPU83_3835(tyrC)
RGA: RGR602_CH03730(tyrC)
RHN: AMJ98_CH04033(tyrC)
RPHA: AMC79_CH04014(tyrC)
RHT: NT26_3431(tyrC)
RHX: AMK02_CH03931(tyrC)
SHZ: shn_17700
BME: BMEI0079
BMEL: DK63_1354
BMEE: DK62_1592
BMF: BAB1_1989
BMB: BruAb1_1964(tyrC)
BABO: DK55_1925
BABR: DO74_2050
BABT: DK49_1682
BABB: DK48_194
BABU: DK53_1910
BABS: DK51_1632
BABC: DO78_1829
BMS: BR1988(tyrC)
BSI: BS1330_I1982(tyrC)
BSF: BSS2_I1922(tyrC)
BSZ: DK67_374
BSV: BSVBI22_A1984(tyrC)
BOV: BOV_1914(tyrC)
BOL: BCOUA_I1988(tyrC)
BCAR: DK60_1966
BCAS: DA85_09550
BMR: BMI_I2011(tyrC)
BPP: BPI_I2048(tyrC)
BPV: DK65_1542
BVL: BF3285c1_0677(tyrC)
OAN: Oant_0992
OAH: DR92_534
BJA: bll1396(tyrC)
BRA: BRADO6464(tyrC)
BBT: BBta_1182(tyrC)
BRS: S23_63970(tyrC)
AOL: S58_11590
BRAD: BF49_3262
BRO: BRAD285_6366(tyrC)
RPA: RPA4440(tyrC)
RPB: RPB_4255
RPC: RPC_4284
RPD: RPD_4102
RPE: RPE_4343
RPT: Rpal_4928
NWI: Nwi_0582
NHA: Nham_0673
OCA: OCAR_4772
OCG: OCA5_c31800(tyrC)
OCO: OCA4_c31280(tyrC)
VGO: GJW-30_1_00717(tyrA)
BHE: BH16210(tyrC)
BHN: PRJBM_01608(tyrC)
BHS: BM1374165_01676(tyrC)
BQU: BQ13130(tyrC)
BQR: RM11_1208
BTR: BT_2597(tyrC)
BTX: BM1374166_02242(tyrC)
BGR: Bgr_19820(tyrC)
BVN: BVwin_14710(tyrC)
XAU: Xaut_0393
AZC: AZC_4618
SNO: Snov_3470
MEX: Mext_1592
MDI: METDI2257
MCH: Mchl_1873
MET: M446_5258
MPO: Mpop_1647
MNO: Mnod_5818
MOR: MOC_2277
META: Y590_07445
MAQU: Maq22A_1p32200(tyrA)
BID: Bind_0308
MSL: Msil_1209
HDN: Hden_2762
RVA: Rvan_3049
PHL: KKY_2952
BVR: BVIR_155
MSC: BN69_0656
MMED: Mame_02217(tyrC)
MCG: GL4_0021
HDI: HDIA_4356(tyrC)
RBM: TEF_02050
CCR: CC_2224
CAK: Caul_3229
CSE: Cseg_2876
SIL: SPO3176
RSP: RSP_6215
RCP: RCAP_rcc02982(tyrA)
JAN: Jann_1035
RDE: RD1_3387(tyrC)
RLI: RLO149_c027460(tyrC)
PDE: Pden_1408
DSH: Dshi_2945(tyrC)
KVU: EIO_0915
KVL: KVU_0442(tyrC)
KRO: BVG79_00703(tyrC)
PSF: PSE_0145
PGA: PGA1_c25230(tyrC)
PGL: PGA2_c23230(tyrC)
PGD: Gal_00869
PHP: PhaeoP97_02393(tyrC)
PPIC: PhaeoP14_02309(tyrC)
OAT: OAN307_c40620(tyrC)
OAR: OA238_c05170(tyrC)
OTM: OSB_06200
PTP: RCA23_c21030(tyrC)
CID: P73_3660
MALG: MALG_02792
RSU: NHU_00398
RHC: RGUI_1421
SPSE: SULPSESMR1_02431(tyrA)
RMM: ROSMUCSMR3_01256(tyrA)
LVS: LOKVESSMR4R_00454(tyrA)
AHT: ANTHELSMS3_01141(tyrA)
HNE: HNE_3400
HBA: Hbal_0228
ZMO: ZMO0420
ZMN: Za10_0826
ZMM: Zmob_0955
ZMB: ZZ6_0835
ZMI: ZCP4_0855
ZMC: A265_00845(tyrC)
ZMR: A254_00845(tyrC)
NAR: Saro_0696
SAL: Sala_2888
SPHP: LH20_20755
SMAZ: LH19_23735
SGI: SGRAN_4158(tyrC)
SWI: Swit_3007
SPHM: G432_10455
STAX: MC45_14300
SPHI: TS85_19710
SSAN: NX02_07520
SPKC: KC8_14280
SPHD: HY78_10455
SSY: SLG_02140
SPMI: K663_00485
SPHB: EP837_01366(tyrC)
SPHR: BSY17_1335
SINB: SIDU_15170
SPHT: K426_00505
SFLA: SPHFLASMR4Y_02396(tyrA)
BLAS: BSY18_3219
ELI: ELI_11420
AAY: WYH_02768
ADO: A6F68_00750(tyrA_1)
GOX: GOX2251
GOH: B932_2751
ACR: Acry_0440
GDI: GDI1627(tyrA)
GDJ: Gdia_1832
GXY: GLX_17400
GXL: H845_3222
KEU: S101446_02256(tyrC)
APK: APA386B_1690(tyrA)
ASZ: ASN_2215(tyrC)
RRU: Rru_A3263
RRF: F11_16720
RCE: RC1_4086(tyrA)
MAG: amb3975
MGY: MGMSRv2__4164(tyrC)
MAGX: XM1_1375(tyrC)
MAGN: WV31_14985
ALI: AZOLI_p40654(tyrC)
ABS: AZOBR_p1130164(tyrC)
TMO: TMO_0139(tyrC)
TXI: TH3_17765
MAGQ: MGMAQ_2974(tyrA)
AGL: PYTT_1757
VBL: L21SP4_01018(tyrC)
MOX: DAMO_1205(tyrC)
 » show all
Taxonomy
Reference
1  [PMID:4206476]
  Authors
Stenmark SL, Pierson DL, Jensen RA, Glover GI.
  Title
Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway.
  Journal
Nature 247:290-2 (1974)
Reference
2  [PMID:7419490]
  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
J Bacteriol 144:247-57 (1980)
Reference
3
  Authors
Byng, G., Whitaker, R., Flick, C. and Jensen, R.A.
  Title
Enzymology of L-tyrosine biosynthesis in corn (Zea mays).
  Journal
Phytochemistry 20:1289-1292 (1981)
Reference
4  [PMID:3967752]
  Authors
Mayer E, Waldner-Sander S, Keller B, Keller E, Lingens F.
  Title
Purification of arogenate dehydrogenase from Phenylobacterium immobile.
  Journal
FEBS Lett 179:208-12 (1985)
DOI:10.1016/0014-5793(85)80519-6
Reference
5
  Authors
Lingens, F., Keller, E. and Keller, B.
  Title
Arogenate dehydrogenase from Phenylobacterium immobile.
  Journal
Methods Enzymol 142:513-518 (1987)
Reference
6  [PMID:2972718]
  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
IUBMB Enzyme Nomenclature: 1.3.1.43
ExPASy - ENZYME nomenclature database: 1.3.1.43
BRENDA, the Enzyme Database: 1.3.1.43
CAS: 64295-75-6

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