Literature summary for 4.2.3.152 extracted from

Spence, E.; Bryan, S.J.; Lisfi, M.; Cullum, J.; Dunlap, W.C.; Shick, J.M.; Mullineaux, C.W.; Long, P.F.
2-epi-5-epi-Valiolone synthase activity is essential for maintaining phycobilisome composition in the cyanobacterium Anabaena variabilis ATCC 29413 when grown in the presence of a carbon source (2013), Photosynth. Res., 116, 33-43.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Trichormus variabilis	-	-	-

Synonyms

Synonyms	Comment	Organism
EVS	-	Trichormus variabilis

General Information

General Information	Comment	Organism
malfunction	in-frame complete deletion of the 2-epi-5-epi-valiolone synthase gene has little effect on in vivo production of shinorine. Complete segregation of the 2-epi-5-epi-Valiolone synthase gene deletion mutant proves difficult and is achieved only when the mutant is grown in the dark and in a medium supplemented with fructose. The segregated mutant shows a striking colour change from native bluegreen to pale yellow-green, corresponding to substantial loss of the photosynthetic pigment phycocyanin, as evinced by combinations of absorbance and emission spectra. Transcriptional analysis of the mutant grown in the presence of fructose under dark or light conditions reveals downregulation of the cpcA gene that encodes the alpha subunit of phycocyanin, whereas the gene encoding nblA, a protease chaperone essential for phycobilisome degradation, is not expressed	Trichormus variabilis
metabolism	2-epi-5-epi-valiolone synthase activity is essential for maintaining phycobilisome composition in the cyanobacterium Anabaena variabilis ATCC 29413 when grown in the presence of a carbon source	Trichormus variabilis

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Release 2023.1 (January 2023)