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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Organization of six functional mouse alcohol dehydrogenase genes on two overlapping bacterial artificial chromosomes.

Mammalian alcohol dehydrogenases (ADH) form a complex enzyme system based on amino-acid sequence, functional properties, and gene expression pattern. At least four mouse Adh genes are known to encode different enzyme classes that share less than 60% amino-acid sequence identity. Two ADH-containing and overlapping C57BL/6 bacterial artificial chromosome clones, RP23-393J8 and -463H24, were identified in a library screen, physically mapped, and sequenced. The gene order in the complex and two new mouse genes, Adh5a and Adh5b, and a pseudogene, Adh5ps, were obtained from the physical map and sequence. The mouse genes are all in the same transcriptional orientation in the order Adh4-Adh1-Adh5a-Adh5b-Adh5ps- Adh2- Adh3. A phylogenetic tree analysis shows that adjacent genes are most closely related suggesting a series of duplication events resulted in the gene complex. Although mouse and human ADH gene clusters contain at least one gene for ADH classes I-V, the human cluster contains 3 class I genes while the mouse cluster has two class V genes plus a class V pseudogene.[1]

References

  1. Organization of six functional mouse alcohol dehydrogenase genes on two overlapping bacterial artificial chromosomes. Szalai, G., Duester, G., Friedman, R., Jia, H., Lin, S., Roe, B.A., Felder, M.R. Eur. J. Biochem. (2002) [Pubmed]
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