Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and its expression in E. coli

Peter Penzes, Xianshu Wang, Zuzana Sperkova, Joseph L. Napoli*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


Peptides sequenced from the purified rat liver cytosolic retinal dehydrogenase P1 were used to design oligonucleotides for cloning its cDNA. The deduced amino acid sequence of P1, now designated retinal dehydrogenase type I or Ra1DH(I), has close similarity with mouse AHD-2 and rat kidney aldehyde dehydrogenase, but is distinct from rat phenobarbital-inducible aldehyde dehydrogenase (PIADH), the presumed rat liver homolog of mouse AHD-2. Rat kidney (100%) and lung (88%) show relatively high mRNA levels of Ra1DH(I), liver (34%) and brain (22%) have moderate levels, and testis (8%) has low levels. Retinoid status affects Ra1DH(I) mRNA levels differently in different tissues. E. coli-expressed Ra1DH(I) exhibits allosteric kinetics for retinal with a Hill coefficient of 1.7, K0.5 value of 1.4 μM and a V(max) of 52 nmol min-1 mg-1 protein. These data establish the cospecificity of P1 and Ra1DH(I), show that retinoid status affects expression of its mRNA in a tissue-dependent manner, and illustrate that aldehyde dehydrogenase isozymes with extensive homology can participate in different metabolic paths, e.g., Ra1DH vs. PIADH.

Original languageEnglish (US)
Pages (from-to)167-172
Number of pages6
Issue number2
StatePublished - Jun 3 1997


  • Aldehyde dehydrogenase
  • Liver dehydrogenase
  • Retinaldehyde
  • Retinoic acid
  • Retinoid

ASJC Scopus subject areas

  • Genetics


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