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Article

Thermodynamic and mutational studies of l-N-carbamoylase from Sinorhizobium meliloti CECT 4114 catalytic centre.

Biochimie - 1 Jul 2006

Martínez-Rodríguez Sergio, Andújar-Sánchez Montserrat, Clemente Jiménez Josefa María, Jara-Pérez Vicente, Rodríguez-Vico Felipe, Las Heras-Vázquez Francisco Javier

Abstract excerpt

Purified site-directed mutants of Sinorhizobium meliloti CECT 4114 l-N-carbamoylase (SmLcar) in which Glu132, His230, Asn279 and Arg292 were replaced have been studied by kinetic methods and isothermal titration calorimetry (ITC). The importance of His230, Asn279 and Arg292 residues in the recogn...

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Identifiers

PMID: 16519985
DOI: 10.1016/j.biochi.2006.01.012

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16519985-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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