Razdan K, Heinrikson R L, Zurcher-Neely H, Morris P W, Anderson L E
Department of Biological Sciences, University of Illinois, Chicago 60680.
Arch Biochem Biophys. 1992 Oct;298(1):192-7. doi: 10.1016/0003-9861(92)90112-a.
Two cDNAs which correspond to two very similar Class I aldolases have been isolated from a pea (Pisum sativum L.) cDNA library. With the exception of one codon they match the experimentally determined N-terminal sequence of a pea chloroplast aldolase. The deduced C-terminal sequence of one of these clones is unique among Class I aldolases. The deduced C-terminus of the other is more like the C-terminus of other eucaryotic Class I aldolases. Comparisons of sequence homology suggest that the pea chloroplast isozymes are only marginally more closely related to the anaerobically induced plant aldolases than to aldolases from animals.
从豌豆(Pisum sativum L.)cDNA文库中分离出了两个与两种非常相似的I类醛缩酶相对应的cDNA。除了一个密码子外,它们与实验确定的豌豆叶绿体醛缩酶的N端序列相匹配。这些克隆之一推导的C端序列在I类醛缩酶中是独特的。另一个推导的C端更类似于其他真核生物I类醛缩酶的C端。序列同源性比较表明,豌豆叶绿体同工酶与厌氧诱导的植物醛缩酶的亲缘关系仅略高于与动物醛缩酶的亲缘关系。