Abstract:
:The first prokaryotic urea carboxylase has previously been purified and characterized from Oleomonas sagaranensis. As the results indicated the presence of an ATP-dependent urea degradation pathway in Bacteria, the characterization of the second component of this pathway, allophanate hydrolase, was carried out. The gene encoding allophanate hydrolase was found adjacent to the urea carboxylase gene. The purified, recombinant enzyme exhibited ammonia-generating activity towards allophanate, and, together with urea carboxylase, efficiently produced ammonia from urea in an ATP-dependent manner. The substrate specificity of the enzyme was strict, and analogs of allophanate were not hydrolyzed. Moreover, although the urea carboxylase exhibited carboxylase activity towards urea, acetamide, and formamide, ammonia-releasing activity of the two enzymes combined was detected only towards urea, indicating that the pathway was specific for urea degradation.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Kanamori T,Kanou N,Kusakabe S,Atomi H,Imanaka Tdoi
10.1016/j.femsle.2005.02.023keywords:
subject
Has Abstractpub_date
2005-04-01 00:00:00pages
61-5issue
1eissn
0378-1097issn
1574-6968pii
S0378-1097(05)00118-7journal_volume
245pub_type
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