Urease, a nickel-containing metalloenzyme, was the first enzyme to be crystallized and has a prominent position in the history of biochemistry. In the present study, we identified a nickel urease gene cluster, ureABCEFGDH, in Bacillus paralicheniformis ATCC 9945a and characterized it in Escherichia coli Enzymatic assays demonstrate that this oxygen-stable urease is also an iron-containing acid urease. Heterologous expression assays of UreH suggest that this accessory protein is involved in the transmembrane transportation of nickel and iron ions. Moreover, this iron-containing acid urease has a potential application in the degradation of urea in rice wine. The present study not only enhances our understanding of the mechanism of activation of urease but also provides insight into the evolution of metalloenzymes.IMPORTANCE An iron-containing, oxygen-stable acid urease from B. paralicheniformis ATCC 9945a with good enzymatic properties was characterized. This acid urease shows activities toward both urea and ethyl carbamate. After digestion with 6 U/ml urease, approximately 92% of the urea in rice wine was removed, suggesting that this urease has great potential in the food industry.

译文

:脲酶,一种含镍的金属酶,是第一个被结晶的酶,在生物化学史上占有重要地位。在本研究中,我们在副芽孢杆菌ATCC 9945a中鉴定了镍脲酶基因簇ureABCEFGDH,并在大肠杆菌中对其进行了表征。酶法测定表明,该氧稳定脲酶也是一种含铁的酸性脲酶。 UreH​​的异源表达测定表明该辅助蛋白与镍和铁离子的跨膜运输有关。此外,这种含铁的酸性脲酶在米酒中尿素的降解中具有潜在的应用。本研究不仅增进了我们对脲酶激活机理的理解,而且为金属酶的发展提供了见识。重要特征表征了副枝芽孢杆菌ATCC 9945a具有良好的酶学性质的含铁,氧稳定的酸性脲酶。该酸性脲酶显示出对脲和氨基甲酸乙酯的活性。用6 U / ml尿素酶消化后,黄酒中约有92%的尿素被去除,这表明该尿素酶在食品工业中具有巨大的潜力。

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