Hirakawa Yoshihisa, Hanawa Yutaka, Yoneda Kohei, Suzuki Iwane
Faculty of Life and Environmental Sciences, University of Tsukuba, Japan.
FEBS Lett. 2022 Dec;596(23):3051-3059. doi: 10.1002/1873-3468.14475. Epub 2022 Aug 30.
Carbonic anhydrases (CAs) are a universal enzyme family that catalyses the interconversion of carbon dioxide and bicarbonate, and they are localized in most compartments including mitochondria and plastids. Thus far, eight classes of CAs (α-, β-, γ-, δ-, ζ-, η-, θ- and ι-CA) have been characterized. This study reports an interesting gene encoding a fusion protein of β-CA and ι-CA found in the haptophyte Isochrysis galbana. Recombinant protein assays demonstrated that the C-terminal ι-CA region catalyses CO hydration, whereas the N-terminal β-CA region no longer exhibits enzymatic activity. Considering that haptophytes generally have mitochondrion-localized β-CAs and plastid-localized ι-CAs, the fusion CA would show an intermediate stage in which mitochondrial β-CA is replaced by ι-CA in a haptophyte species.
碳酸酐酶(CAs)是一类普遍存在的酶家族,催化二氧化碳和碳酸氢根的相互转化,它们存在于包括线粒体和质体在内的大多数细胞区室中。到目前为止,已鉴定出八类碳酸酐酶(α-、β-、γ-、δ-、ζ-、η-、θ-和ι-碳酸酐酶)。本研究报道了在金藻等鞭金藻中发现的一个有趣的基因,该基因编码一种β-碳酸酐酶和ι-碳酸酐酶的融合蛋白。重组蛋白分析表明,ι-碳酸酐酶的C末端区域催化CO水合作用,而β-碳酸酐酶的N末端区域不再表现出酶活性。考虑到金藻通常有线粒体定位的β-碳酸酐酶和质体定位的ι-碳酸酐酶,这种融合碳酸酐酶将显示出一个中间阶段,即在一种金藻物种中,线粒体β-碳酸酐酶被ι-碳酸酐酶取代。