MetaCyc Enzyme: allantoate amidohydrolase

Species: Phaseolus vulgaris

An allantoate degrading enzyme has been partially purified from developing fruits of Phaseolus vulgaris, and is the first such enzyme to be purified from a plant [Raso07].

The enzyme, which was purified 22-fold, produced ammonia and not urea, suggesting that it is an allantoate amidohydrolase. Surprisingly, ammonia was found in low amounts, about 10% of the amount of S-ureidoglycolate produced. The reason for this in not known.

Enzymatic activity depended on phenylhydrazine,which acted as an activator at low concentrations. EDTA inhibited activity completely, and this inhibition was reversed by manganese, suggesting Mn2+ is a cofactor.

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Created 13-Nov-2007 by Caspi R , SRI International

Enzymatic reaction of: allantoate amidohydrolase

EC Number:

allantoate + 2 H+ + H2O <=> S-ureidoglycine + ammonium + CO2

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 allantoin degradation in plants , allantoin degradation to glyoxylate III , allantoin degradation to ureidoglycolate II (ammonia producing)

The specific activity of the partially purified enzyme was 364 U/mg protein [Raso07].

Cofactors or Prosthetic Groups: Mn2+ [Raso07]

Activators (Allosteric): phenylhydrazine [Raso07]

Inhibitors (Other): EDTA [Raso07]

T(opt): 37 °C [Raso07]

pH(opt): 7 [Raso07]


Raso07: Raso MJ, Munoz A, Pineda M, Piedras P (2007). "Biochemical characterisation of an allantoate-degrading enzyme from French bean (Phaseolus vulgaris): the requirement of phenylhydrazine." Planta 226(5);1333-42. PMID: 17594111

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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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