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Catalytic analysis of a recombinant D-hydantoinase from Agrobacterium tumefaciens
dc.contributor.author | Clemente Jiménez, Josefa María | |
dc.contributor.author | Las Heras Vázquez, Francisco Javier | |
dc.contributor.author | Martínez Rodríguez, Sergio | |
dc.contributor.author | Mingorance Cazorla, Lydia | |
dc.contributor.author | de la Escalera-Hueso S | |
dc.contributor.author | Rodríguez Vico, Felipe | |
dc.date.accessioned | 2024-05-22T11:57:32Z | |
dc.date.available | 2024-05-22T11:57:32Z | |
dc.date.issued | 2003 | |
dc.identifier.issn | 0141-5492 | |
dc.identifier.uri | http://hdl.handle.net/10835/16541 | |
dc.description.abstract | The D-hydantoinase gene of a wild strain of Agrobacterium tumefaciens BQL9 had 99.78% nucleotide sequence identity with other available Agrobacterium genes. The resulting amino acid sequence showed two important substitutions affecting two α-helixes in the secondary structure of the protein. The union of Mn2+ to the protein was essential for activating the enzyme and was independent of the temperature. D-Hydantoinase only was inactivated in the presence of 70 mM EDTA and at over 40 ◦C. The enzyme showed both hydantoinase and pyrimidinase activities, but only with the D-enantiomers of the substrates. Activity was greater for substrates with apolar groups in the number 5 carbon atom of the hydantoin. The native structure of the N-terminal end of this D-hydantoinase proved to be indispensable to its enzymatic activity. | es_ES |
dc.language.iso | en | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Agrobacterium | es_ES |
dc.subject | amino acids | es_ES |
dc.subject | expression | es_ES |
dc.subject | D-hydantoinase | es_ES |
dc.title | Catalytic analysis of a recombinant D-hydantoinase from Agrobacterium tumefaciens | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |