Abstract：
:A d-carbamoylase from Sinorhizobium morelens S-5 was purified and characterized. The enzyme was purified 189-fold to homogeneity with a yield of 19.1% by aqueous two-phase extraction and two steps of column chromatography. The enzyme is a homotetramer with a native molecular mass of 150 kDa and a subunit relative molecular mass of 38 kDa. The optimum pH and temperature of the enzyme were pH 7.0 and 60 degrees C, respectively. The enzyme showed high thermal and oxidative stability. It was found to have a K(m) of 3.76 mM and a V(max) of 383 U/mg for N-carbamoyl-d-p-hydroxyphenylglycine. The hyuC gene coding for this enzyme was cloned, and its nucleotide sequence was determined. The deduced amino acid sequence encoded by the hyuC gene exhibited high homology to the amino acid sequences of d-carbamoylase from other sources. The gene could be highly expressed in Escherichia coli, and the product was purified to homogeneity from the recombinant. Our results show that the enzyme has great potential for industrial application.
journal_name
Biochimiejournal_title
Biochimieauthors
Wu S,Liu Y,Zhao G,Wang J,Sun Wdoi
10.1016/j.biochi.2005.05.013keywords:
subject
Has Abstractpub_date
2006-03-01 00:00:00pages
237-44issue
3-4eissn
0300-9084issn
1638-6183pii
S0300-9084(05)00233-6journal_volume
88pub_type
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