AI Article Synopsis
- The enzyme N-Carbamoyl-β-alanine amidohydrolase (Atβcar) from Agrobacterium tumefaciens shows versatility by hydrolyzing various amino acid derivatives to produce different types of amino acids.
- A promiscuity index of 0.54 suggests that Atβcar is moderately promiscuous, particularly effective in hydrolyzing N-carbamoyl-amino acids to produce α-amino acids.
- Research involving mutagenesis and other techniques indicates that residues W218 and A359 play a role in the enzyme's flexibility by influencing the key residue R291, which is essential for its catalytic function.
Article Abstract
The availability of enzymes with a high promiscuity/specificity relationship permits the hydrolysis of several substrates with a view to obtaining a certain product or using one enzyme for several productive lines. N-Carbamoyl-β-alanine amidohydrolase from Agrobacterium tumefaciens (Atβcar) has shown high versatility to hydrolyze different N-carbamoyl-, N-acetyl- and N-formyl-amino acids to produce different α, β, γ and δ amino acids. We have calculated the promiscuity index for the enzyme, obtaining a value of 0.54, which indicates that it is a modestly promiscuous enzyme. Atβcar presented the highest probability of hydrolysis for N-carbamoyl-amino acids, being the enzyme more efficient for the production of α-amino acids. We have also demonstrated by mutagenesis, modelling, kinetic and binding experiments that W218 and A359 indirectly influence the plasticity of the enzyme due to interaction with the environment of R291, the key residue for catalytic activity.
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| http://dx.doi.org/10.1016/j.jchromb.2011.04.008 | DOI Listing |
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