Os05g0101600

Annotated Information

Function

Being by far the largest family of enzymes to support plant metabolism, the cytochrome P450s (CYPs) constitute an excellent reporter of metabolism architecture and evolution. The huge superfamily of CYPs found in angiosperms is built on the successful evolution of 11 ancestral genes, with very different fates and progenies. Essential functions in the production of structural components (membrane sterols), light harvesting (carotenoids) or hormone biosynthesis kept some of them under purifying selection, limiting duplication and sub/neofunctionalization

Expression

Cytochrome P450s (CYPs) are heme-thiolate proteins, most of which catalyze NADPH- and O2-dependent hydroxylation reactions. P450s form a vast superfamily of genes that have been found in bacteria, insects, fish, mammals, plants, and fungi (Chapple, 1998). The nomenclature of P450s is based on amino acid sequence similarity. It assigns proteins with more than 40% identity into the same family, and proteins with more than 55% identity into the same subfamily (Werck-Reichhart and Feyereisen, 2000). Genomes of higher plants contain large number of P450s. For example, the Arabidopsis thaliana genome encodes 246 full-length P450s, accounting for approximately 1% of Arabidopsis gene complement.

Evolution

CYP genes represent around 1% of the plant protein-coding genes, a proportion only outranked and approached by genes coding for regulatory proteins and some families of transcription

Labs working on this gene

Department of Biochemistry, Biophysics, & Molecular Biology, Iowa State University, Ames, IA 50011, USA Rice Functional Genomics Group, Temasek Life Sciences Laboratory, National University of Singapore French National Centre for Scientific Research, Université Paris-Sud, France Department of Molecular Sciences and Center of Excellence in Genomics and Bioinformatics, University of Tennessee, Memphis Department of Plant Stress Response, Institute of Plant Molecular Biology

References

Akashi, T., Aoki, T., and Ayabe, S. (1998). Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett. 431, 287-290. Chapple, C. (1998). Molecular-Genetic Analysis of Plant Cytochrome P450-Dependent Monooxygenases. Annu Rev Plant Physiol Plant Mol Biol 49, 311-343.