Collart F R, Osipiuk J, Trent J, Olsen G J, Huberman E
Center for Mechanistic Biology and Biotechnology, Argonne National Laboratory, IL 60439, USA.
Gene. 1996 Oct 3;174(2):217-20. doi: 10.1016/0378-1119(96)00045-5.
We have cloned and characterized the gene encoding inosine monophosphate dehydrogenase (IMPDH) from Arabidopsis thaliana (At). The transcription unit of the At gene spans approximately 1900 bp and specifies a protein of 503 amino acids with a calculated relative molecular mass (M(r)) of 54,190. The gene is comprised of a minimum of four introns and five exons with all donor and acceptor splice sequences conforming to previously proposed consensus sequences. The deduced IMPDH amino-acid sequence from At shows a remarkable similarity to other eukaryotic IMPDH sequences, with a 48% identity to human Type II enzyme. Allowing for conservative substitutions, the enzyme is 69% similar to human Type II IMPDH. The putative active-site sequence of At IMPDH conforms to the IMP dehydrogenase/guanosine monophosphate reductase motif and contains an essential active-site cysteine residue.
我们已经克隆并鉴定了来自拟南芥(At)的编码肌苷单磷酸脱氢酶(IMPDH)的基因。At基因的转录单元跨度约为1900 bp,编码一个由503个氨基酸组成的蛋白质,计算相对分子质量(M(r))为54,190。该基因至少由四个内含子和五个外显子组成,所有供体和受体剪接序列均符合先前提出的共有序列。从At推导的IMPDH氨基酸序列与其他真核生物IMPDH序列具有显著相似性,与人类II型酶的同一性为48%。考虑到保守取代,该酶与人类II型IMPDH的相似性为69%。At IMPDH的推定活性位点序列符合IMP脱氢酶/鸟苷单磷酸还原酶基序,并包含一个必需的活性位点半胱氨酸残基。