Global InformationArogenate dehydratase information
| Arogenate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 The crystal structure of Cyclohexadienyl dehydratase precursor from Pseudomonas aeruginosa PA01. The secondary structure is displayed in the image, and the residue important for catalysis has been highlighted. | |||||||||
| Identifiers | |||||||||
| EC no. | 4.2.1.91 | ||||||||
| CAS no. | 76600-70-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Arogenate dehydratase (ADT) (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction
- L-arogenate → L phenylalanine + H2O + CO2
Certain forms of the protein have the potential to catalyze a second reaction,[1]
- L-prephenate → L-phenylpyruvate + H2O + CO2
This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis (an example structure is shown to the right.[2]
- ^ Fischer R, Jensen R (1987). "[59] Arogenate dehydratase". Metabolism of Aromatic Amino Acids and Amines. Methods in Enzymology. Vol. 142. pp. 495–502. doi:10.1016/S0076-6879(87)42061-2. ISBN 9780121820428. PMID 3600377.
{{cite book}}:|journal=ignored (help) - ^ Tan K, Marshall N, Buck K, Joachimiak A (2009). "The crystal structure of cyclohexadienyl dehydratase precursor from Pseudomonas aeruginosa PA01". doi:10.2210/pdb3kbr/pdb.
{{cite journal}}: Cite journal requires|journal=(help)