Sokolov A P, Trotsenko Y A
Biokhimiia. 1978 May;43(5):782-8.
3-Hexulosephosphate synthase (HPS), the key enzyme of the hexulosephosphate cycle of formaldehyde fixation, was isolated from facultative methylotroph Pseudomonas oleovorans. Enzyme was purified 100-fold. The purification procedure involved fractionation with ammonium sulfate, gel-filtration on Sephadex G-150 and chromatography on DEAE-Sephadex A-50. The purified enzyme gave single band on analytical polyacrylamide gel electrophoresis. Optimal conditions for activity of HPS are: pH 7,0, temperature 50 degrees C. The molecular weight was calculated to be 45 000 from gel-filtration experiments. HPS is active only in the presence of Mg2+ or Mn2+. Ribulose-5-phosphate is the sole acceptor of formaldehyde. Activity of the enzyme is inhibited by NADH and NADPH.
3-己酮糖磷酸合酶（HPS）是甲醛固定化己酮糖磷酸循环的关键酶，它是从兼性甲基营养菌食油假单胞菌中分离出来的。该酶被纯化了100倍。纯化过程包括硫酸铵分级分离、Sephadex G-150凝胶过滤和DEAE-Sephadex A-50柱层析。纯化后的酶在分析型聚丙烯酰胺凝胶电泳上呈现单一条带。HPS的最佳活性条件为：pH 7.0，温度50℃。通过凝胶过滤实验计算出其分子量为45000。HPS仅在Mg2+或Mn2+存在时具有活性。5-磷酸核酮糖是甲醛的唯一受体。该酶的活性受到NADH和NADPH的抑制。
