4.5 Article

Cloning and characterization of a novel human homolog of mouse U26, a putative PQQ-dependent AAS dehydrogenase

Journal

MOLECULAR BIOLOGY REPORTS
Volume 32, Issue 1, Pages 47-53

Publisher

SPRINGER
DOI: 10.1007/s11033-003-2716-4

Keywords

2-aminoadipic 6-semialdehyde dehydrogenase; AMP-binding domain; phosphopantetheine-binding domain; PQQ-binding domain; RT-PCR

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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.

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