Article · Wikipedia archive · Last revised Jul 27, 2026

Arogenic acid

Arogenic acid is an intermediate in the biosynthesis of phenylalanine and tyrosine. At physiological pH it exists as its conjugate base arogenate as the acid form is unstable.

Last revised
Jul 27, 2026
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≈ 1 min
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330 w
Citations
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Source
Wikipedia ↗
Arogenic acid
source ↗
Structure of L-Arogenate
Names
IUPAC name
1-[(2S)-2-amino-2-carboxyethyl]-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid
Other names
(1s,4s)-1-(2-Amino-2-carboxyethyl)-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid
Identifiers
3D model (JSmol)
4458841
ChEBI
ChemSpider
KEGG
UNII
  • InChI=1S/C10H13NO5/c11-7(8(13)14)5-10(9(15)16)3-1-6(12)2-4-10/h1-4,6-7,12H,5,11H2,(H,13,14)(H,15,16)/p-1/t6?,7-,10?/m0/s1
    Key: MIEILDYWGANZNH-DSQUFTABSA-M
  • C1=CC(C=CC1O)(CC(C(=O)[O-])N)C(=O)O
  • Zwitterion: C1=CC(C=CC1O)(CC(C(=O)[O-])[NH3+])C(=O)[O-]
Properties
C10H13NO5
Molar mass 227.216 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

Arogenic acid is an intermediate in the biosynthesis of phenylalanine and tyrosine. At physiological pH it exists as its conjugate base arogenate as the acid form is unstable.

Metabolism

Arogenate is synthesized from prephenate by transamination. This reaction can be catalyzed by several enzymes, including aromatic-amino-acid transaminase,1 aspartate—prephenate aminotransferase2 and glutamate—prephenate aminotransferase:3

prephenate + amino acid → arogenate + keto acid

The amino acid in this case can be either aspartate or glutamate, which turn into oxaloacetate and 2-oxoglutarate, respectively.

Arogenate is then turned into either phenylalanine or tyrosine. When prephenate dehydratase4 or arogenate dehydratase5 act upon arogenate, phenylalanine is produced:

arogenate → phenylalanine + H2O + CO2

When arogenate dehydrogenase,6 arogenate dehydrogenase (NAD(P)+)7 or arogenate dehydrogenase (NADP+)8 acts upon arogenate, tyrosine is produced:910

2D representation of the chemical structure of Q27125430.
L-arogenate
+ NAD+
 
 
 
CO2
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
CO2
 
2D representation of the chemical structure of tyrosine.
L-tyrosine
+ NADH
 


References

References

  1. "ENZYME - 2.6.1.57 aromatic-amino-acid transaminase". enzyme.expasy.org. Retrieved 2024-03-05.
  2. "ENZYME - 2.6.1.78 aspartate--prephenate aminotransferase". enzyme.expasy.org. Retrieved 2024-03-05.
  3. "ENZYME - 2.6.1.79 glutamate--prephenate aminotransferase". enzyme.expasy.org. Retrieved 2024-03-05.
  4. "ENZYME - 4.2.1.51 prephenate dehydratase". enzyme.expasy.org. Retrieved 2024-03-05.
  5. "ENZYME - 4.2.1.91 arogenate dehydratase". enzyme.expasy.org. Retrieved 2024-03-05.
  6. "ENZYME - 1.3.1.43 arogenate dehydrogenase". enzyme.expasy.org. Retrieved 2024-03-05.
  7. "ENZYME - 1.3.1.79 arogenate dehydrogenase [NAD(P)(+)]". enzyme.expasy.org. Retrieved 2024-03-05.
  8. "ENZYME - 1.3.1.78 arogenate dehydrogenase (NADP(+))". enzyme.expasy.org. Retrieved 2024-03-05.
  9. Stenmark SL, Pierson DL, Jensen RA, Glover GI (1974). "Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway". Nature. 247 (439): 290–2. Bibcode:1974Natur.247..290S. doi:10.1038/247290a0. PMID 4206476. S2CID 4200115.
  10. Byng G, Whitaker R, Flick C, Jensen RA (1981). "Enzymology of L-tyrosine biosynthesis in corn (Zea mays)". Phytochemistry. 20 (6): 1289–1292. Bibcode:1981PChem..20.1289B. doi:10.1016/0031-9422(81)80023-4.