McFadden B A, Schuster E
J Bacteriol. 1972 Feb;109(2):751-6. doi: 10.1128/jb.109.2.751-756.1972.
Phosphoglycerate kinase levels in Hydrogenomonas facilis were reasonably constant whether cells were utilizing or synthesizing hexose during growth. Specific enzyme activities (micromoles of 3-phosphoglycerate disappearing per minute per milligram of protein) at 30 C were 0.234, 0.391, 0.300, and 0.229 in the "soluble" fraction derived from cells grown on fructose, lactate, succinate, and glutamate, respectively. The enzyme was purified 300-fold from succinate-grown cells. The final preparation, which was not homogenous but was free from glyceraldehyde-3-phosphate dehydrogenase and adenylate kinase, had a specific activity at 30 C of 90 mumoles of 3-phosphoglycerate per min per mg of protein. K(m) values for adenosine triphosphate (ATP), 3-phosphoglycerate, and Mg(++) were 0.16, 0.83, and 0.4 mm, respectively, at pH 7.4 and 30 C. Adenosine monophosphate (AMP) inhibited 23% at a ratio of AMP to ATP of 2.4, and the possible physiological implications of this inhibition are discussed. No evidence was found for an enzyme which catalyzes ATP-dependent conversion of 3-phosphoglycerate to 1,3-diphosphoglycerate, AMP, and phosphate.
在嗜氢假单胞菌中，无论细胞在生长过程中是利用还是合成己糖，磷酸甘油酸激酶的水平都相当稳定。在30℃时，分别以果糖、乳酸、琥珀酸和谷氨酸为碳源培养的细胞所提取的“可溶性”部分中，特定酶活性（每分钟每毫克蛋白质中3 - 磷酸甘油酸消失的微摩尔数）分别为0.234、0.391、0.300和0.229。该酶从以琥珀酸为碳源培养的细胞中纯化了300倍。最终制备物虽不均一，但不含甘油醛 - 3 - 磷酸脱氢酶和腺苷酸激酶，在30℃时其比活性为每毫克蛋白质每分钟90微摩尔3 - 磷酸甘油酸。在pH 7.4和30℃条件下，三磷酸腺苷（ATP）、3 - 磷酸甘油酸和镁离子（Mg++）的米氏常数（K(m)）分别为0.16、0.83和0.4毫摩尔。当一磷酸腺苷（AMP）与ATP的比例为2.4时，AMP抑制作用达23%，并讨论了这种抑制作用可能的生理意义。未发现催化ATP依赖的3 - 磷酸甘油酸转化为1,3 - 二磷酸甘油酸、AMP和磷酸的酶的证据。
