Abstract
The conformationally restricted phenylalanine analogue 2-aminoindan-2-phosphonic acid (AIP) inhibits phenylalanine ammonia-lyase (PAL) competitively in a time-dependent manner. This phenomenon was investigated in more detail with the heterologously expressed, highly purified homotetrameric PAL-1 isozyme from parsley. The kinetic analysis revealed that the enzyme-inhibitor complex is formed in a single “slow” step with an association rate of k 2=2.6±0.04 10 4 M −1 s −1. The inhibition is reversible with a dissociation rate of k −2=1.8±0.04 10 −4 s −1 and an equilibrium constant of K i=7±2 nM. The previously described PAL inhibitor (S)-2-aminooxy-3-phenylpropanoic acid [ (S)-AOPP] was also found to be a slow-binding inhibitor of PAL-1. The carboxyl analogue of AIP, 2-aminoindan-2-carboxylic acid, served as a substrate of PAL-1 and was converted to indene-2-carboxylic acid.
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