頁籤選單縮合
題名 | Characterization of a Putative Pseudomonas UDPglucose Pyrophosphorylase=假單胞桿菌尿嘧啶雙磷酸葡萄糖聚磷酸化酶之生化分析 |
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作者 | 張晃猷; 黃秀珍; 李靜嫺; 彭慧玲; | 書刊名 | Proceedings of the National Science Council : Part B, Life Science |
卷期 | 23:2 1999.04[民88.04] |
頁次 | 頁74-84 |
分類號 | 361.1925 |
關鍵詞 | 假單胞桿菌; 尿嘧啶雙磷酸葡萄糖聚磷酸化酶; GalU; Gor; Pseudomonas sp.; UDPglucose pyrophosphorylase; |
語文 | 英文(English) |
英文摘要 | A UDP-glucose pyrophosphorylase encoding gene was identified through functional complementation screen ing by using an Escherichia coli galU mutant. Sequence analysis of the gene indicated that it is most likely derived from a Pseud monas sp. The gene is located immediately up stream and transcribed in the same direction of the gor (glutathione reductase) gene and is capable of encoding a protein 30,943 daltons in size. The gene product synthesized in Escherichia coli was purified and its biochemical properties characterized. The recombinant UDP-glucose pyrophosphorylase exhibited a molecular weight of 130 kDa, suggesting a tetrameric organization of the gene product. Two mutant forms of the enzyme were identified. The activity of the mutant enzyme with a tyrosine to histidine (Y26 lH) substitution was found to be greatly reduced. On the other hand, the tyrosine to cysteine (Y84C) substitution resulted in an enzyme that functions normally at 37 ? but rather poorly at temperatures lower than 30 ?. |
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