Louwrier, A. and Knowles, C.J. (1996) The purification and characterization of a novel D(-)-specific carbamoylase enzyme from an Agrobacterium sp. Enzyme and Microbial Technology, 19 (8). pp. 562-571. ISSN 0141-0229.
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A carbamoylase enzyme was purified from a cell-free extract of Agrobacterium sp. with an overall yield of 81%. It was judged to be homogenous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with a subunit molecular weight of 38,000 daltons. Further studies on the native enzyme suggested that the active enzyme was present as a dimer, with a pl of 5.5. It was able to cleave a variety of N-carbamoyl substrates, but was strictly D(-) specific. It was found to have a K-m of 0.82 mM and a V-max of 31 U mg(-1) for D(-) N-carbamoyl hydroxyphenylglycine in the presence of 10 mM dithiothreitol. It showed no metal ion requirements but was inhibited by iodoacetic acid and iodoacetamide, both thiol reagents. The N-terminal amino acid sequence of the enzyme was elucidated.
|Uncontrolled keywords:||carbamoylase; hydantoinase; N-carbamoyl hydroxyphenylglycine; hydroxyphenylglycine; hydroxyphenyl hydantoin|
|Subjects:||Q Science > QR Microbiology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||F.D. Zabet|
|Date Deposited:||29 Jun 2009 10:08|
|Last Modified:||29 Jun 2009 10:08|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/18649 (The current URI for this page, for reference purposes)|
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