MetaCyc Enzyme: arogenate dehydratase

Species: Nicotiana sylvestris

Gene-Reaction Schematic

Gene-Reaction Schematic

Enzymatic reaction of: arogenate dehydratase

Inferred from experiment

EC Number:

L-arogenate + H+ → CO2 + L-phenylalanine + H2O

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of L-phenylalanine and L-tyrosine biosynthesis, L-phenylalanine biosynthesis II

The enzyme activity of N. silvestris arogenate dehydratase is inhibited by phenylalanine and activated by tyrosine. The maximum activation was observed at 0.25 mM of tyrosine. Zn2+ or Cu2+ at 2.5 mM completely abolished the enzyme activity, and Co2+ reduced the activity by 50%, whereas Mg2+ and Mn2+ had no effects at the same concentration.

The optimum temperature is 32 oC. The optimum pH is between 8.5 and 9.5.

Activators (Allosteric): L-tyrosine [Jung86] Inhibitors (Unknown Mechanism): L-phenylalanine [Jung86], Zn2+ [Jung86], Cu2+ [Jung86], Co2+ [Jung86]

Primary Physiological Regulators of Enzyme Activity: L-tyrosine, L-phenylalanine

Kinetic Parameters:
Substrate Km (μM) Citations
L-arogenate 300.0 [Jung86]


Jung86: Jung E, Zamir LO, Jensen RA (1986). "Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate." Proc Natl Acad Sci U S A 83(19);7231-5. PMID: 3463961

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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