PUBLICATION

Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A

Authors
Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E., and von Lintig, J.
ID
ZDB-PUB-010417-11
Date
2001
Source
The Journal of biological chemistry   276(17): 14110-14116 (Journal)
Registered Authors
Lampert, Johanna
Keywords
none
MeSH Terms
  • Cloning, Molecular
  • Tissue Distribution
  • Drosophila/enzymology
  • Animals
  • Phylogeny
  • Female
  • Time Factors
  • Drosophila Proteins
  • beta Carotene/chemistry*
  • beta Carotene/metabolism
  • Phenotype
  • Retinaldehyde/chemistry
  • Models, Chemical
  • Mass Spectrometry
  • Expressed Sequence Tags
  • Carotenoids/chemistry
  • Carotenoids/metabolism
  • Zebrafish
  • RNA/metabolism
  • Terpenes/chemistry
  • Sequence Homology, Amino Acid
  • Humans
  • Male
  • Oxygen/metabolism*
  • DNA, Complementary/metabolism
  • Gene Library
  • Mice
  • Molecular Sequence Data
  • Oxygenases/chemistry*
  • Oxygenases/metabolism
  • Vitamin A/chemistry
  • Vitamin A/metabolism*
  • Chromatography, High Pressure Liquid
  • Catalysis
  • Norisoprenoids*
  • beta-Carotene 15,15'-Monooxygenase
  • Amino Acid Sequence
  • Mice, Inbred BALB C
(all 38)
PubMed
11278918 Full text @ J. Biol. Chem.
Abstract
In vertebrates, symmetric versus asymmetric cleavage of b-carotene in the biosynthesis of vitamin A and its derivatives has been controversially discussed. Recently we have been able to identify a cDNA encoding a metazoan b,b-carotene-15,15'-dioxygenase from the fruit fly Drosophila melanogaster. This enzyme catalyzes the key step in vitamin A biosynthesis, symmetrically cleaving b-carotene to give two molecules of retinal. Mutations in the corresponding gene are known to lead to a blind, vitamin A deficient phenotype. Orthologs of this enzyme have very recently also been found in vertebrates and molecularly characterized. Here we report the identification of a cDNA from mouse encoding a second type of carotene dioxygenase catalyzing exclusively the asymmetric oxidative cleavage of b-carotene at the 9',10' double bond of b-carotene and resulting in the formation of b-apo-10'-carotenal and b-ionone, a substance known as a floral scent from, e.g., roses. Besides b-carotene, lycopene is also oxidatively cleaved by the enzyme. The deduced amino acid sequence shares significant sequence identity with the b,b-carotene-15,15'-dioxygenases and the two enzyme types have several conserved motifs. To establish its occurrence in different vertebrates, we then attempted and succeeded in cloning cDNAs encoding this new type of carotene dioxygenase from human and zebrafish as well. As regards their possible role, the apocarotenals formed by this enzyme may be the precursors for the biosynthesis of retinoic acid or exert unknown physiological effects. Thus, in contrast to Drosophila, in vertebrates both symmetric and asymmetric cleavage pathways exist for carotenes, revealing a greater complexity of carotene metabolism here.
Genes / Markers
Figures
No images available
Expression
Phenotype
No data available
Mutations / Transgenics
No data available
Human Disease / Model
No data available
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
No data available
Mapping
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Citation
Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E., and von Lintig, J. (2001) Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. The Journal of biological chemistry. 276(17):14110-14116.