Susskind B M, Warren L G, Reeves R E
Biochem J. 1982 Apr 15;204(1):191-6. doi: 10.1042/bj2040191.
Isotope studies indicate that hexose-to-pentose interconversion by axenic Entamoeba histolytica conserves the C-1 and C-6 hexose carbon atoms. Transketolase was readily identified in amoebal extracts, and transaldolase could not be demonstrated. However, sedoheptulose 7-phosphate is a substrate for the PPi-dependent amoebal phosphofructokinase, and sedoheptulose 1,7-bisphosphate is cleaved by amoebal aldolase to dihydroxyacetone phosphate and erythrose phosphate. Since these three enzymes catalyse physiologically reversible reactions, a non-oxidative pathway for hexose-pentose interconversion exists in amoebae in the absence of transaldolase. By using known amoebal enzyme, the conversion of ribose into fructose was confirmed in vitro. Some kinetic parameters of amoebal phosphofructokinase, transketolase and aldolase were determined.
同位素研究表明,无菌培养的溶组织内阿米巴将己糖转化为戊糖的过程中,己糖的C-1和C-6碳原子得以保留。在阿米巴提取物中很容易鉴定出转酮醇酶,但未证实有转醛醇酶。然而,景天庚酮糖7-磷酸是依赖焦磷酸的阿米巴磷酸果糖激酶的底物,景天庚酮糖1,7-二磷酸被阿米巴醛缩酶裂解为磷酸二羟丙酮和磷酸赤藓糖。由于这三种酶催化生理上可逆的反应,因此在没有转醛醇酶的情况下,阿米巴存在一条非氧化的己糖-戊糖相互转化途径。通过使用已知的阿米巴酶,在体外证实了核糖向果糖的转化。测定了阿米巴磷酸果糖激酶、转酮醇酶和醛缩酶的一些动力学参数。