Choy F Y, Lee Y P
Can J Biochem Cell Biol. 1983 Dec;61(12):1292-303. doi: 10.1139/o83-166.
Sugar phosphate phosphohydrolase was purified approximately 500- to 600-fold to apparent homogeneity from Escherichia coli B, Escherichia coli C, Escherichia coli var. communior, Escherichia acidilactici, Enterobacter aerogenes, Neisseria meningitidis, and Saccharomyces cereviseae. The molecular weights of the enzyme as estimated by gel filtration ranged from 97 X 10(3) to 101 X 10(3). The enzyme was composed of two subunits with the same molecular weight which ranged from 50 X 10(3) to 52 X 10(3), as determined by sodium dodecyl sulfate gel electrophoresis. Homogeneous enzyme preparations hydrolyse all the tested alpha-D-aldohexose 1-phosphate, D-(keto or aldo)hexose 6-phosphate, and pentose phosphate substrates significantly. When the microorganisms were transferred from growth medium with 1% glucose to that without glucose, there were dramatic increases in both the specific and total enzyme activities. At least three isozymes appeared to be present in S. cereviseae, and two appeared to be present in E. coli B, E. coli var. communior, and N. meningitidis. Rabbit antiserum immunized against sugar phosphate phosphohydrolase purified from E. coli B cross-reacted with both the crude extracts and purified preparations of the enzyme from the other microorganisms. The presence of neither sugar phosphate phosphohydrolase activity nor immunocrossreacting material was detected in the following microorganisms: Aspergillus niger, Azotobacter chroococcum, Bacillus subtilis, Bacillus pumilis, Citrobacter freundii, Clostridium butyricum, Corynebacterium xerosis, Flavobacterium aquatile, Flavobacterium synxanthum, Lactobacillus bulgaricus, Micrococcus coralinus, Neisseria perflava, Neurospora crassa, Penicilium expansum, Penicilium notatum, Proteus mirabilis, Proteus vulgaris, Pseudomonas fluorescens, Saccharomyces fermenti, Sarcina lutea, and Streptomyces antibioticus. At present, no conclusive relationship can be established between the phosphoenolpyruvate phosphotransferase system and the enzyme sugar phosphate phosphohydrolase among microorganisms. The physiological role of sugar phosphate phosphohydrolase as a transferase and regulatory enzyme is discussed.
从大肠杆菌B、大肠杆菌C、普通大肠杆菌变种、嗜酸乳杆菌、产气肠杆菌、脑膜炎奈瑟菌和酿酒酵母中纯化得到磷酸糖磷酸水解酶，纯化倍数约为500至600倍，达到表观均一性。通过凝胶过滤法估算，该酶的分子量在97×10³至101×10³之间。经十二烷基硫酸钠凝胶电泳测定，该酶由两个分子量相同的亚基组成，分子量范围在50×10³至52×10³之间。均一的酶制剂能显著水解所有测试的α-D-醛己糖1-磷酸、D-（酮或醛）己糖6-磷酸和戊糖磷酸底物。当微生物从含1%葡萄糖的生长培养基转移至不含葡萄糖的培养基时，比酶活和总酶活均显著增加。酿酒酵母中似乎至少存在三种同工酶，大肠杆菌B、普通大肠杆菌变种和脑膜炎奈瑟菌中似乎存在两种同工酶。用从大肠杆菌B纯化的磷酸糖磷酸水解酶免疫的兔抗血清与其他微生物的酶粗提物和纯化物均发生交叉反应。在以下微生物中未检测到磷酸糖磷酸水解酶活性或免疫交叉反应物质：黑曲霉、褐球固氮菌、枯草芽孢杆菌、短小芽孢杆菌、弗氏柠檬酸杆菌、丁酸梭菌、干燥棒状杆菌、水生黄杆菌、黄色黄杆菌、保加利亚乳杆菌、珊瑚微球菌、全黄奈瑟菌、粗糙脉孢菌、扩展青霉、点青霉、奇异变形杆菌、普通变形杆菌、荧光假单胞菌、发酵酿酒酵母、藤黄八叠球菌和抗生链霉菌。目前，在微生物中磷酸烯醇丙酮酸磷酸转移酶系统与磷酸糖磷酸水解酶之间无法建立确凿的关系。文中讨论了磷酸糖磷酸水解酶作为转移酶和调节酶的生理作用。
