Structure of dihydropyrimidinase from Sinorhizobium meliloti CECT4114: New features in an amidohydrolase family member
Identifiers
Share
Metadata
Show full item recordAuthor/s
Martínez Rodríguez, Sergio![University of Almería authority University of Almería authority](/themes/Mirage2/images/autoridades/autoridad.png)
![University of Almería authority University of Almería authority](/themes/Mirage2/images/autoridades/autoridad.png)
![University of Almería authority University of Almería authority](/themes/Mirage2/images/autoridades/autoridad.png)
![University of Almería authority University of Almería authority](/themes/Mirage2/images/autoridades/autoridad.png)
Date
2010Abstract
The recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114 (SmelDhp) has been characterised and its crystal structure elucidated at 1.85 Å. The global architecture of the protein is reminiscent of that of the amidohydrolase superfamily, consisting of two domains; an (a/b)8 TIM-like barrel domain, where the catalytic centre is located, and a smaller b-sheet sandwich domain of unknown function.
The c-terminal tails of each subunit extend toward another monomer in a swapping-like manner, creating a hydrogen bond network which suggests its implication in protein oligomerisation. Mutational and structural evidence suggest the involvement of a conserved tyrosine in the reaction mechanism of the enzyme. SmelDhp presents both hydantoinase and dihydropyrimidinase activities, with higher affinity for the natural six-membered ring substrates. For the five-membered ring substrates, affinity was greater for those with aliphatic and apolar groups in the 5th carbon atom, with the hig...
Palabra/s clave
Dihydropyrimidinase
Hydantoinase
Hydantoinase process
Amino acid production
Amidohydrolase superfamily