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MetaCyc Enzyme: arogenate dehydratase

Species: Nicotiana sylvestris

Gene-Reaction Schematic: ?

Gene-Reaction Schematic


Enzymatic reaction of: arogenate dehydratase

EC Number: 4.2.1.91

L-arogenate + H+ <=> CO2 + L-phenylalanine + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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

Summary:
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]


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Fri Sep 4, 2015, biocyc13.