Biochemical and Mutational Characterization of N-Succinyl- Amino Acid Racemase from Geobacillus stearothermophilus CECT49
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Soriano Maldonado, Pablo; Andújar Sánchez, Montserrat; Clemente Jiménez, Josefa María; Rodríguez Vico, Felipe; Las Heras Vázquez, Francisco Javier; [et al.]Fecha
2015Resumen
N-Succinyl-amino acid racemase (NSAAR), long referred to as N-acyl- or N-acetyl-amino acid racemase, is an enolase superfamily member whose biotechnological potential was discovered decades ago, due to its use in the industrial dynamic kinetic resolution methodology first known as ‘‘Acylase Process’’. In previous works, an extended and enhanced substrate spectrum of the NSAAR from Geobacillus kaustophilus CECT4264 toward different N-substituted amino acids was reported. In this work, we describe the cloning, purification, and characterization of the NSAAR from Geobacillus stearothermophilus CECT49 (GstNSAAR). The enzyme has been
extensively characterized, showing a higher preference toward N-formyl-amino acids than to N-acetyl-amino acids, thus confirming that the use of the former substrates is more appropriate for a biotechnological application of the enzyme. The enzyme showed an apparent thermal denaturation midpoint of 77.0 ± 0.1 C and an apparent molecular mass of 184 ± 5 kDa, ...
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N-Succinyl-amino acid racemase
N-Acylamino acid racemase
N-Acetyl-amino acid racemase
Acylase process
Amino acid
Racemase
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