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

Mol Biol Rep. 2005 Mar;32(1):47-53. doi: 10.1007/s11033-003-2716-4.

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.

MeSH terms

  • Aldehyde Dehydrogenase
  • Aldehyde Oxidoreductases / genetics*
  • Animals
  • Base Sequence
  • Cells, Cultured
  • Cloning, Molecular
  • Gene Expression
  • Humans
  • L-Aminoadipate-Semialdehyde Dehydrogenase
  • Mice
  • Molecular Sequence Data
  • Neoplasm Proteins / biosynthesis
  • Neoplasm Proteins / genetics*
  • PQQ Cofactor / genetics
  • Proteins / genetics
  • RNA, Messenger / analysis
  • RNA, Messenger / metabolism
  • Sequence Analysis, DNA
  • Sequence Analysis, Protein
  • Tissue Distribution

Substances

  • Neoplasm Proteins
  • Proteins
  • RNA, Messenger
  • U26 protein, mouse
  • PQQ Cofactor
  • Aldehyde Oxidoreductases
  • Aldehyde Dehydrogenase
  • AASDH protein, human
  • L-Aminoadipate-Semialdehyde Dehydrogenase

Associated data

  • GENBANK/AY314787