Dimroth P, Eggerer H
Proc Natl Acad Sci U S A. 1975 Sep;72(9):3458-62. doi: 10.1073/pnas.72.9.3458.
Citrate lyase [EC 4.1.3.6; citrate oxaloacetate-lyase (pro-3S-CH2-COO--leads to acetate)] from Klebsiella aerogenes has been dissociated with urea; the three different subunits, alpha-chain (molecular weight congruent to 54,000), beta-chain (molecular weight congruent to 32,000), and gamma-chain (acyl carrier protein; molecular weight congruent to 10,000), have been isolated in pure and catalytically active state. Recombination of the three subunits produced citrate lyase that was indistinguishable from the untreated enzyme. The alpha-chain in the presence of acetyl-S-acyl carrier protein catalyzed the formation of the corresponding citryl thioester with liberation of acetate, and the beta-chain catalyzed the cleavage of citryl-S-acyl carrier protein with liberation of oxaloacetate. A simple enzymic method for the preparation of citryl-S-acyl carrier protein is described.
产气克雷伯菌中的柠檬酸裂解酶[EC 4.1.3.6；柠檬酸草酰乙酸裂解酶（pro-3S-CH2-COO-→乙酸盐）]已用尿素解离；三种不同的亚基，α链（分子量约为54,000）、β链（分子量约为32,000）和γ链（酰基载体蛋白；分子量约为10,000），已被分离成纯的且具有催化活性的状态。这三个亚基重组产生的柠檬酸裂解酶与未处理的酶无法区分。在乙酰-S-酰基载体蛋白存在下，α链催化形成相应的柠檬酰硫酯并释放出乙酸盐，β链催化柠檬酰-S-酰基载体蛋白的裂解并释放出草酰乙酸。本文描述了一种制备柠檬酰-S-酰基载体蛋白的简单酶法。
