Shao Z, Newman E B
Biology Dept., Concordia University, Montreal, Quebec, Canada.
Eur J Biochem. 1993 Mar 15;212(3):777-84. doi: 10.1111/j.1432-1033.1993.tb17718.x.
The sdaB gene which codes for the second L-serine deaminase (L-SD) of Escherichia coli K-12 has been sequenced and shown to be very similar to the sdaA gene which codes for the first L-serine deaminase. sdaB is transcribed in rich medium, particularly in the absence of glucose, and is under the control of catabolite activator protein. A mutation which established expression of the sdaB gene and synthesis of L-serine deaminase 2 in minimal medium has been demonstrated to result in a change in the ribosome-binding site of the sdaB gene.
编码大肠杆菌K-12第二种L-丝氨酸脱氨酶（L-SD）的sdaB基因已被测序，结果显示它与编码第一种L-丝氨酸脱氨酶的sdaA基因非常相似。sdaB在丰富培养基中被转录，尤其是在没有葡萄糖的情况下，并且受分解代谢物激活蛋白的控制。已证明在基本培养基中使sdaB基因表达并合成L-丝氨酸脱氨酶2的一个突变导致了sdaB基因核糖体结合位点的改变。
