The partial purification and properties of a phytoene synthesizing enzyme system

Maudinas, Bernard; Bucholtz, Michael L.; Papastephanou, Constantin; Katiyar, Sarvagya S.; Briedis, Anita V.; Porter, John W.

doi:10.1016/0003-9861(77)90049-2

Cited by 64 publications

(35 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presence of several genes encoding putative GGDS enzymes in most plants (www.phytozome.net) suggests that different isozymes might be involved in the production of specific groups of isoprenoids (including carotenoids). Consistent with this possibility, multi-enzyme complexes harboring GGDS and PSY activities to directly convert IPP into phytoene have been isolated from chromoplasts (Islam et al, 1977;Maudinas et al, 1977;Camara, 1993;Fraser et al, 2000). Additionally supporting a role for specific GGDS isoforms in channeling precursors to the carotenoid pathway, statistical testing of the correlation between carotenoid content and candidate gene transcript levels in a maize germplasm collection revealed that the expression of genes encoding DXS, DXR, HDR, and only one of the three plastidial GGDS enzymes positively correlated with endosperm carotenoid content .…”

Section: Mep Pathway To Ggppmentioning

confidence: 92%

Carotenoid Biosynthesis in Arabidopsis: A Colorful Pathway

Ruiz-Sola

Rodríguez‐Concepción

2012

The Arabidopsis Book

467

372

View full text Add to dashboard Cite

Plant carotenoids are a family of pigments that participate in light harvesting and are essential for photoprotection against excess light. Furthermore, they act as precursors for the production of apocarotenoid hormones such as abscisic acid and strigolactones. In this review, we summarize the current knowledge on the genes and enzymes of the carotenoid biosynthetic pathway (which is now almost completely elucidated) and on the regulation of carotenoid biosynthesis at both transcriptional and post-transcriptional levels. We also discuss the relevance of Arabidopsis as a model system for the study of carotenogenesis and how metabolic engineering approaches in this plant have taught important lessons for carotenoid biotechnology.

show abstract

Section: Mep Pathway To Ggppmentioning

confidence: 92%

Carotenoid Biosynthesis in Arabidopsis: A Colorful Pathway

Ruiz-Sola

Rodríguez‐Concepción

2012

The Arabidopsis Book

467

372

View full text Add to dashboard Cite

show abstract

“…Carotenoids are found on envelope and thylakoid membranes, implying that either the pathway forms on two membrane sites or that carotenoids are transported by an unknown mechanism. Carotenoid metabolons (enzyme complexes) are predicted to exist on the basis of high molecular weight complexes containing PSY or other carotenoid enzymes (Maudinas et al, 1977;Camara et al, 1982;Kreuz et al, 1982;Al-Babili et al, 1996;Bonk et al, 1997;Lopez et al, 2008). A recent study showed that the capacity for enzymes to interact was associated with enhanced carotenoid pathway activity (Quinlan et al, 2012).…”

Section: Open Questions On Metabolon Organization and Dynamicsmentioning

confidence: 99%

Plastid Localization of the Key Carotenoid Enzyme Phytoene Synthase Is Altered by Isozyme, Allelic Variation, and Activity

et al. 2012

View full text Add to dashboard Cite

Plant carotenoids have unique physiological roles related to specific plastid suborganellar locations. Carotenoid metabolic engineering could enhance plant adaptation to climate change and improve food security and nutritional value. However, lack of fundamental knowledge on carotenoid pathway localization limits targeted engineering. Phytoene synthase (PSY), a major rate-controlling carotenoid enzyme, is represented by multiple isozymes residing at unknown plastid sites. In maize (Zea mays), the three isozymes were transiently expressed and found either in plastoglobuli or in stroma and thylakoid membranes. PSY1, with one to two residue modifications of naturally occurring functional variants, exhibited altered localization, associated with distorted plastid shape and formation of a fibril phenotype. Mutating the active site of the enzyme reversed this phenotype. Discovery of differential PSY locations, linked with activity and isozyme type, advances the engineering potential for modifying carotenoid biosynthesis.

show abstract

“…The pathway likely functions as a multienzyme complex(es) to facilitate metabolite channeling, as predicted by the absence of pathway intermediates and the presence of complexes containing carotenoid biosynthetic enzymes (Maudinas et al, 1977;Camara et al, 1982;Kreuz et al, 1982;AlBabili et al, 1996;Bonk et al, 1997;Lopez et al, 2008). In this study, we examined an intriguing portion of the pathway, where hydroxylation of rings in carotenes is catalyzed by two structurally distinct enzymes, P450 heme (CYP97) and nonheme diiron (HYD) enzymes DellaPenna, 2001, 2004;Kim and DellaPenna, 2006;Quinlan et al, 2007).…”

mentioning

confidence: 99%

Synergistic Interactions between Carotene Ring Hydroxylases Drive Lutein Formation in Plant Carotenoid Biosynthesis

et al. 2012

View full text Add to dashboard Cite

Plant carotenoids play essential roles in photosynthesis, photoprotection, and as precursors to apocarotenoids. The plastidlocalized carotenoid biosynthetic pathway is mediated by well-defined nucleus-encoded enzymes. However, there is a major gap in understanding the nature of protein interactions and pathway complexes needed to mediate carotenogenesis. In this study, we focused on carotene ring hydroxylation, which is performed by two structurally distinct classes of enzymes, the P450 CYP97A and CYP97C hydroxylases and the nonheme diiron HYD enzymes. The CYP97A and HYD enzymes both function in the hydroxylation of b-rings in carotenes, but we show that they are not functionally interchangeable. The formation of lutein, which involves hydroxylation of both b-and «-rings, was shown to require the coexpression of CYP97A and CYP97C enzymes. These enzymes were also demonstrated to interact in vivo and in vitro, as determined using bimolecular fluorescence complementation and a pull-down assay, respectively. We discuss the role of specific hydroxylase enzyme interactions in promoting pathway flux and preventing the formation of pathway dead ends. These findings will facilitate efforts to manipulate carotenoid content and composition for improving plant adaptation to climate change and/or for enhancing nutritionally important carotenoids in food crops.

show abstract

The partial purification and properties of a phytoene synthesizing enzyme system

Cited by 64 publications

References 20 publications

Carotenoid Biosynthesis in Arabidopsis: A Colorful Pathway

Carotenoid Biosynthesis in Arabidopsis: A Colorful Pathway

Plastid Localization of the Key Carotenoid Enzyme Phytoene Synthase Is Altered by Isozyme, Allelic Variation, and Activity

Synergistic Interactions between Carotene Ring Hydroxylases Drive Lutein Formation in Plant Carotenoid Biosynthesis

Contact Info

Product

Resources

About