Characterization of a cytosolic malate dehydrogenase cdna which encodes an isozyme toward oxaloacetate reduction in wheat
文献类型：期刊论文
| 作者 | Ding, Y; Ma, QH |
| 刊名 | Biochimie
 |
| 出版日期 | 2004-08-01 |
| 卷号 | 86期号:8页码:509-518 |
| 关键词 | Cytosolic malate dehydrogenase Cdna cloning Biochemical analysis Triticum aestivum l |
| ISSN号 | 0300-9084 |
| DOI | 10.1016/j.biochi.2004.07.011 |
| 通讯作者 | Ma, qh(mqh@ibcas.ac.cn) |
| 英文摘要 | Malate dehydrogenase (mdh), which is ubiquitous in nature, catalyzes the interconversion of oxaloacetate and malate. higher plants contain multiple forms of mdh that differ in co-enzyme specificity, subcellular localization and physiological function. cytosolic nad-dependent mdh (cymdh) is one class of mdh that has not been extensively characterized in plants. here we report the cloning of a cdna from wheat by rt-pcr and cdna library screening, which is designated as tamdh. sequence analysis indicated that tamdh exhibits a highly similarity to other plant cymdhs. immunological analysis confirmed that tamdh encoded a cytosolic nad-dependent mdh. the secondary and three-dimensional structures of tamdh were analyzed by molecular modeling. dna gel-blot analyses demonstrated that tamdh gene exists as two copies in the wheat genome. rna and protein gel-blot hybridization indicated that both tamdh mrna and protein were constitutively expressed in vegetative tissues of wheat, with slightly lower levels in roots than in leaves and stems. in silico analysis indicated that tamdh was also expressed in various reproductive tissues and tissues under many different stress conditions. kinetic analysis of bacterially expressed and purified protein confirmed that tamdh catalyzed a reaction driven towards malate synthesis, which is consistent with other cymdhs. evolutionary analysis showed that this class of genes evolved from a very ancestral gene. the cymdh represents an ancestral form of mdh, which is highly conserved in plants, animals and bacteria. this implies that cymdhs are housekeeping genes and may have very essential functions in plant metabolism. (c) 2004 elsevier sas. all rights reserved. |
| WOS关键词 | CRASSULACEAN ACID METABOLISM ; SEQUENCE-ANALYSIS ; PURIFICATION ; PROTEIN ; GENE ; MITOCHONDRIAL ; LOCALIZATION ; ISOENZYMES ; ENZYMES ; CHLOROPLASTS |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000224296100002 |
| 出版者 | EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2376843 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Ma, QH |
| 作者单位 | 1.Chinese Acad Sci, Inst Bot, Key Lab Photosynth & Environm Mol Physiol, Beijing 100093, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ding, Y,Ma, QH. Characterization of a cytosolic malate dehydrogenase cdna which encodes an isozyme toward oxaloacetate reduction in wheat[J]. Biochimie,2004,86(8):509-518. |
| APA | Ding, Y,&Ma, QH.(2004).Characterization of a cytosolic malate dehydrogenase cdna which encodes an isozyme toward oxaloacetate reduction in wheat.Biochimie,86(8),509-518. |
| MLA | Ding, Y,et al."Characterization of a cytosolic malate dehydrogenase cdna which encodes an isozyme toward oxaloacetate reduction in wheat".Biochimie 86.8(2004):509-518. |
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来源：中国科学院大学
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