N-Carbamoyl- -alanine amidohydrolase from Agrobacterium tumefaciens C58: A promiscuous enzyme for the production of amino acids
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Martínez Gómez, Ana Isabel; Andújar Sánchez, Montserrat; Clemente Jiménez, Josefa María; Neira Faleiro, José Luis; Rodríguez Vico, Felipe; [et al.]Fecha
2011Resumen
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- -alanine amidohydrolase from Agrobacterium tumefaciens (At car) has shown high versatility to hydrolyze different N-carbamoyl-, N-acetyl- and N-formyl-amino acids to produce different , , and 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. At car presented the highest probability of hydrolysis for N-carbamoyl-amino acids, being the enzyme more efficient for the production of -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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Binding
Thermodynamics
Circular dichroism
Promiscuity
Elasticity
N-Carbamoyl- -alanine amidohydrolase