Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans

Applied Microbiology and Biotechnology
J OgawaS Shimizu

Abstract

N-Carbamoyl-L-amino acid amidohydrolase was purified to homogeneity for the first time from Alcaligenes xylosoxidans. The enzyme showed high affinity toward N-carbamoyl-L-amino acids with long-chain aliphatic or aromatic substituents, and hydrolyzed those with short-chain substituents quite well. The enzyme hydrolyzed N-formyl- and N-acetylamino acids quickly and very slowly, respectively. The enzyme did not hydrolyze beta-ureidopropionate and ureidosuccinate. The relative molecular mass of the native enzyme was about 135,000 and the enzyme consisted of two identical polypeptide chains. The enzyme activity was significantly inhibited by sulfhydryl reagents and required the following divalent metal ions: Mn2+, Ni2+ and Co2+.

Citations

Oct 16, 2009·Applied Microbiology and Biotechnology·Sergio Martínez-RodríguezFrancisco Javier Las Heras-Vázquez
Dec 5, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Sergio Martínez-RodríguezJose Antonio Gavira
Mar 25, 2006·Bioscience, Biotechnology, and Biochemistry·Jun OgawaSakayu Shimizu
May 21, 2013·Biotechnology and Applied Biochemistry·Hemraj S NandanwarGurinder S Hoondal
Aug 24, 2010·Biotechnology Progress·Joaquín Pozo-DengraFrancisco Javier Las Heras-Vázquez
Oct 29, 2005·Journal of Molecular Microbiology and Biotechnology·Sergio Martínez-RodríguezFrancisco Javier Las Heras-Vázquez
Apr 17, 2013·Biotechnology and Applied Biochemistry·Hemraj S NandanwarGurinder S Hoondal
Oct 1, 1996·Applied and Environmental Microbiology·J OgawaS Shimizu
Mar 8, 2006·Biochimie·Sergio Martínez-RodríguezFrancisco Javier Las Heras-Vázquez

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