McKenzie G H, Ch'ng A L, Gayler K R
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052 Australia.
Plant Physiol. 1979 Mar;63(3):578-82. doi: 10.1104/pp.63.3.578.
The enzymic capacities for ammonia assimilation into amino acids have been investigated in chloroplasts from the siphonous green alga Caulerpa simpliciuscula (Turner) C. Ag. The results show that these chloroplasts differ from those of higher plants in having present simultaneously the enzymic capacities to permit assimilation of ammonia by two pathways. Glutamine synthetase (EC 6.3.1.2) activity at levels up to 4 mumoles per mg chlorophyll per hour were found in soluble extracts of the chloroplasts. Glutamine(amide):alpha-ketoglutarate aminotransferase (oxidoreductase ferredoxin) (EC 1.4.7.1) activity at levels up to 1.4 mumoles per mg chlorophyll per hour was detected by incubation of photosynthetically active chloroplasts either in light or with reduced ferredoxin. Together these enzymes provide the capacity for the conventional pathway of ammonium assimilation in chloroplasts via glutamine. A similar level of a glutamate dehydrogenase with an unusually low K(m) for ammonia which has been described previously in these chloroplasts provides the second potential pathway.
已对管形绿藻简单羽藻(Turner)C. Ag. 的叶绿体中氨同化为氨基酸的酶促能力进行了研究。结果表明,这些叶绿体与高等植物的叶绿体不同,它们同时具备通过两条途径同化氨的酶促能力。在叶绿体的可溶性提取物中发现谷氨酰胺合成酶(EC 6.3.1.2)的活性高达每毫克叶绿素每小时4微摩尔。通过在光照下或与还原型铁氧还蛋白一起孵育光合活性叶绿体,检测到谷氨酰胺(酰胺):α-酮戊二酸氨基转移酶(氧化还原酶铁氧还蛋白)(EC 1.4.7.1)的活性高达每毫克叶绿素每小时1.4微摩尔。这些酶共同提供了叶绿体中通过谷氨酰胺进行铵同化的传统途径的能力。先前在这些叶绿体中描述的一种对氨具有异常低K(m)值的谷氨酸脱氢酶的类似水平提供了第二条潜在途径。