KEGG   ENZYME: 4.2.1.91Help
Entry
EC 4.2.1.91                 Enzyme                                 

Name arogenate dehydratase;
carboxycyclohexadienyl dehydratase;
L-arogenate hydro-lyase (decarboxylating)
Class Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming)
Reaction(IUBMB) L-arogenate = L-phenylalanine + H2O + CO2 [RN:R00691]
Reaction(KEGG) R00691;
(other) R01373
Show
Substrate L-arogenate [CPD:C00826]
Product L-phenylalanine [CPD:C00079];
H2O [CPD:C00001];
CO2 [CPD:C00011]
Comment Also acts on prephenate and D-prephenyllactate. cf. EC 4.2.1.51,
prephenate dehydratase.
Pathway PATH: ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
PATH: ec01061  Biosynthesis of phenylpropanoids
PATH: ec01063  Biosynthesis of alkaloids derived from shikimate
               pathway
PATH: ec01070  Biosynthesis of plant hormones
PATH: ec01100  Metabolic pathways
Orthology KO: K05359  carboxycyclohexadienyl dehydratase
Genes CVI: CV_0224
BVI: Bcep1808_0119
MSM: MSMEG_3442
Taxonomy
Structures PDB: 3KBR  
Reference
  Authors
  Title
  Journal
1  [PMID:3600377]
Fischer R, Jensen R.
Arogenate dehydratase.
Methods. Enzymol. 142 (1987) 495-502.
Reference
  Authors
  Title

  Journal
  Organism
2  [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.
Neurospora crassa [GN:ncr]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:3124763]
Siehl DL, Conn EE.
Kinetic and regulatory properties of arogenate dehydratase in
seedlings of Sorghum bicolor (L.) Moench.
Arch. Biochem. Biophys. 260 (1988) 822-9.
Sorghum bicolor [GN:sbi]
Other DBs ExplorEnz - The Enzyme Database: 4.2.1.91
IUBMB Enzyme Nomenclature: 4.2.1.91
ExPASy - ENZYME nomenclature database: 4.2.1.91
BRENDA, the Enzyme Database: 4.2.1.91
CAS: 76600-70-9

DBGET integrated database retrieval system