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作 者:管玉霞[1]
机构地区:[1]厦门大学细胞生物学研究室
出 处:《厦门大学学报(自然科学版)》1992年第2期182-187,共6页Journal of Xiamen University:Natural Science
摘 要:本工作对钝齿棒状杆菌AS1.542及其产赖氨酸诱变株253(AEC),365-25P-3(AEC,Hosor^-)赖氨酸分枝途径的第一个酶DDP Sase进行初步纯化,研究天门冬系氨基酸对该酶活性的影响,对钝齿棒状杆菌AS1.542的赖氨酸生物合成调节机制进行初步探讨,发现钝齿棒状杆菌AS1.542赖氨酸分枝途径的第一个酶DDP Sase受末端产物赖氨酸的反馈抑制,在诱变株253(AEC),365-25P-3(AEC,Hoser^-)菌中,赖氨酸对DDP Sase的反馈抑制被部分解除,因而有利于产生大量赖氨酸。The work tentatively purified the first enzyme-Dinydrodipicolinate Synthetase (DDP Sase) of the lysine branch path in Corynebacterium crenatum AS1. 542 and mutants 253 (AEC), 365-25P-3CAEC,Hoser-) which produce the lysine. The amino acids of aspartic family affect DDP Sase activity was studied. The regulating function of lysine biosynthesis in Corynebacterium crenatum AS1. 542 was preliminaryly researched. The first enzyme DDP Sase of lysine branch path in Corynebacterium crenatum AS1. 512 inhibited by the end product-iysine was found. Producing a great quantity lysine is due to partly relieve the feedback inhibition of iysine to DDP Sase in mutants 253 (AEC) 365-25P-3(AEC,Hoser-).
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