Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase |
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Authors: | Liu Wang Chaoneng Ji Yiren Xu Jian Xu Jianfeng Dai Qihan Wu Maoqing Wu Xianqiong Zou Liyun Sun Shaohua Gu Yi Xie Yumin Mao |
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Affiliation: | (1) State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai, 200433, Peoples Republic of China |
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Abstract: | Mouse U26 has been defined as a 2-aminoadipic 6-semialdehyde dehydrogenase. It was speculated to be a PQQ-dependent AAS dehydrogenase due to the research of demonstrating PQQ as a new B vitamin. We isolated a novel human cDNA from the human fetal brain cDNA library we constructed. Its deduced protein was most related to mouse U26. Thus, we termed it human U26. This putative protein contains an AMP-binding domain, a Phosphopantetheine-binding domain and six PQQ-binding motifs. Human U26 mRNA is ubiquitously expressed in adult tissues and is highly expressed in colon adenocarcinoma (CX-1) and colon adenocarcinoma (GI-112) cell lines. Further study should be made to clarify the precise function of human U26.The nucleotide sequence reported in this paper has been submitted to GenBank under accession number AY314787. |
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Keywords: | 2-aminoadipic 6-semialdehyde dehydrogenase AMP-binding domain Phosphopantetheine-binding domain PQQ-binding domain RT-PCR |
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