Molecular evolution of urea amidolyase and urea carboxylase in fungi
نویسندگان
چکیده
منابع مشابه
Structure and function of urea amidolyase
Urea is the degradation product of a wide range of nitrogen containing bio-molecules. Urea amidolyase (UA) catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source. It is widely distributed in fungi, bacteria and other microorganisms, and plays an important role in nitrogen recycling in the biosphere. UA is composed of urea carboxylase (UC) a...
متن کاملPurification and properties of the urea amidolyase from Candida utilis.
Urea amidolyase was purified to homogeneity from extracts of Candida utilis. The purification involves protamine sulfate precipitation, ammonium sulfate precipitation, polyethylene glycol precipitation, Sepharose 6B gel filtration, DEAE-cellulose column chromatography, and hydroxylapatite column chromatography. The final preparation is pure as judged by disc-gel electrophoresis. The molecular w...
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Evidence is presented that the enzymes catalyzing the three reactions involved in urea cleavage in Candida utilis, biotin carboxylation, urea carboxylation, and allophanate hydrolysis occur as a complex of enzymes. The allophanate-hydrolyzing activity could not be separated from the urea-cleaving activity using common methods of protein purification. Further, urea cleavage and allophanate hydro...
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Candida utilis contains an inducible enzyme, urea amidolyase, which catalyzes the decomposition of urea with formation of carbon dioxide and ammonia. This reaction is accompanied by the cleavage of ATP with liberation of equimolar amounts of ADP and inorganic phosphate, is strictly dependent for activity on divalent (Mg++ or Mn++) and monovalent (K+, Rb+, Csf, or NH4+) cations, and requires cat...
متن کاملEnzymatic characterization of a prokaryotic urea carboxylase.
We identified the first prokaryotic urea carboxylase (UCA) from a member of the alpha subclass of the class Proteobacteria, Oleomonas sagaranensis. This enzyme (O. sagaranensis Uca) was composed of 1,171 amino acids, and its N-terminal region resembled the biotin carboxylase domains of various biotin-dependent carboxylases. The C-terminal region of the enzyme harbored the Met-Lys-Met motif foun...
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ژورنال
عنوان ژورنال: BMC Evolutionary Biology
سال: 2011
ISSN: 1471-2148
DOI: 10.1186/1471-2148-11-80