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植物和藻类碳酸酐酶的化学性质、分布及生理学特性

Chemical properties, distribution, and physiology of plant and algal carbonic anhydrases.

作者信息

Graham D, Reed M L, Patterson B D, Hockley D G, Dwyer M R

出版信息

Ann N Y Acad Sci. 1984;429:222-37. doi: 10.1111/j.1749-6632.1984.tb12340.x.

Abstract

Plant carbonic anhydrases (CAs) have a range of molecular weights (MW). Among flowering plants, dicotyledons with C3 photosynthesis have two isoenzymes of 140-250K each with 6 subunits, while monocotyledons have two isoenzymes of 42-45K. Plant and animal CAs have a similar amino acid content, subunit size and zinc content, suggesting they are homologous proteins, although the higher plant CAs have no esterase activity and are not strongly inhibited by sulfonamides. Algal CAs vary widely in MW and some are highly sensitive to sulfonamides like the animal enzymes. The two plant isoenzymes, from the chloroplast and cytosol, can be separated by gradient polyacrylamide gel electrophoresis and subsequently visualized by enzymic H+ ion production. In plants, CAs probably facilitate diffusion of CO2 to the site of photosynthetic fixation; they may also have a role in pH regulation, in the use of bicarbonate by aquatic plants and in concentrating inorganic carbon within the chloroplast.

摘要

植物碳酸酐酶(CAs)具有一系列分子量(MW)。在开花植物中,进行C3光合作用的双子叶植物有两种同工酶,每种分子量为140 - 250K,各有6个亚基,而单子叶植物有两种分子量为42 - 45K的同工酶。植物和动物的碳酸酐酶具有相似的氨基酸含量、亚基大小和锌含量,这表明它们是同源蛋白,尽管高等植物的碳酸酐酶没有酯酶活性,也不会被磺胺类药物强烈抑制。藻类碳酸酐酶的分子量差异很大,有些像动物酶一样对磺胺类药物高度敏感。来自叶绿体和细胞质的两种植物同工酶可以通过梯度聚丙烯酰胺凝胶电泳分离,随后通过酶促产生H⁺离子来显现。在植物中,碳酸酐酶可能促进二氧化碳扩散到光合固定的部位;它们也可能在pH调节、水生植物利用碳酸氢盐以及在叶绿体内浓缩无机碳方面发挥作用。

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