Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis

Author:

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

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference37 articles.

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2. Biocatalysis to amino acid-based chiral pharmaceuticals—Examples and perspectives;Bommarius;J. Mol. Catal., B Enzym.,1998

3. Production of optically pure d- and l-α-amino acids by bioconversion of D, l-5-monosubstituted hydantoin derivatives;Syldatk;Adv. Biochem. Eng. Biotechnol.,1990

4. Complete conversion of d,l-5-monosubstituted hydantoins with a low velocity of chemical racemization into d-amino acids using whole cells of recombinant Escherichia coli;Martinez-Rodriguez;Biotechnol. Prog.,2002

5. S. Martinez-Rodriguez, J.M. Clemente-Jimenez, F. Rodriguez-Vico, F.J. Las Heras-Vazquez, Activity measurement of hydantoin racemase enzyme: a key for the production of optically pure d-amino acids, in: R. Konno, N. Fujii, H. Homma, H. Brückner, G. Fisher, A. D'Aniello (Eds.), d-amino acids: a new frontier in: amino acid and protein research Nova Science, Inc., Hauppauge, New York, USA (in press).

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