Literature summary for 1.3.1.33 extracted from

Shi, C.; Shi, X.
Characterization of three genes encoding the subunits of light-independent protochlorophyllide reductase in Chlorella protothecoides CS-41 (2006), Biotechnol. Prog., 22, 1050-1055.

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Organism

Organism	UniProt	Comment	Textmining
Auxenochlorella protothecoides	-	enzyme components protein L, protein N and protein B are all transcribed constitutively independent of illumination and presence of glucose. Steady-state amounts of proteins in the light-grown cells are two- to threefold greater than in dark-grown cells. Approximately the same amount of protein is present in cultures grown mixtrophically or heterotrophically both containing glucose. Much less protein is present in photoautotrophic cells. Therefore light-independent enzyme activity depends on post-transcriptional and post-translational regulation and switches on both in light and dark	-
Auxenochlorella protothecoides CS-41	-	enzyme components protein L, protein N and protein B are all transcribed constitutively independent of illumination and presence of glucose. Steady-state amounts of proteins in the light-grown cells are two- to threefold greater than in dark-grown cells. Approximately the same amount of protein is present in cultures grown mixtrophically or heterotrophically both containing glucose. Much less protein is present in photoautotrophic cells. Therefore light-independent enzyme activity depends on post-transcriptional and post-translational regulation and switches on both in light and dark	-

Synonyms

Synonyms	Comment	Organism
light-independent protochlorophyllide oxidoreductase	-	Auxenochlorella protothecoides
LIPOR	-	Auxenochlorella protothecoides

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Release 2023.1 (January 2023)