RGD Reference Report - Kinetic properties of chimeric class I aldehyde dehydrogenases for retinal isomers. - Rat Genome Database
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Kinetic properties of chimeric class I aldehyde dehydrogenases for retinal isomers.

Authors: Brodeur, H  Chagnon, S  Parisotto, M  Mader, S  Bhat, PV 
Citation: Brodeur H, etal., Biochem Cell Biol. 2006 Oct;84(5):799-804.
RGD ID: 2306320
Pubmed: (View Article at PubMed) PMID:17167544
DOI: Full-text: DOI:10.1139/o06-038

Retinal dehydrogenase type 1 (RALDH1) catalyzes the oxidation of all-trans and 9-cis retinal to the respective retinoic acids (RAs), whereas another member of the aldehyde dehydrogenase (ALDH) family, the phenobarbital-induced aldehyde dehydrogenase (PB-ALDH), is very poorly active. We have previously generated chimeras between these 2 enzymes that displayed selectivity for retinal isomers in crude bacterial extracts. Here we have characterized the kinetic properties of the corresponding purified recombinant proteins. The all-trans selective chimera RALDH-131 converted all-trans retinal to all-trans RA with 2.9-fold lower efficiency than the wild-type RALDH1 and had only residual activity with 9-cis retinal. The converse chimera PB-131 was specific for 9-cis retinal, with no residual activity for all-trans retinal. MgCl2 inhibited the activities of RALDH1 and PB-131, but not of RALDH-131, suggesting that amino acids 132-510 in RALDH are necessary for inhibition by MgCl2. These data demonstrate that the chimeric enzymes act as retinal isomer-selective ALDHs, and suggest that these enzymes may be useful to study the roles of cis RA isomers in embryogenesis and differentiation in vivo.


Gene Ontology Annotations    

Biological Process

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Aldh1a1  (aldehyde dehydrogenase 1 family, member A1)

Additional Information