Homology modeling of the three membrane proteins of the dhurrin metabolon: Catalytic sites, membrane surface association and protein–protein interactions

Jensen, Kenneth; Osmani, Sarah A.; Hamann, Thomas; Naur, Peter; Møller, Birger Lindberg

doi:10.1016/j.phytochem.2011.05.001

Cited by 35 publications

(32 citation statements)

References 76 publications

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“…Sorghum (subfamily Panicoideae) produces the cyanogenic glycoside dhurrin by modifying the amino acid tyrosine (Poulton 1990). The biosynthetic pathway is short, consisting of two cytochromes P450, a UDP-glycose-glycosyltransferase, and a NADPH-cytochrome P450 reductase, which together form a membrane-bound biosynthetic complex or metabolon (Jensen et al 2011;Nielsen et al 2008). The complex has been transferred to Arabidopsis, which then produces dhurrin, confirming the functional importance of the pathway (Tattersall et al 2001).…”

Section: Derivatives Of Amino Acids (Tryptophan Phenylalanine Tyrosmentioning

confidence: 99%

Flowering Plants. Monocots

Kellogg

2015

203

230

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Section: Derivatives Of Amino Acids (Tryptophan Phenylalanine Tyrosmentioning

confidence: 99%

Flowering Plants. Monocots

Kellogg

2015

203

230

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“…In the related biosynthetic pathway of dhurrin (structure not shown), a cyanogenic glucoside from Sorghum bicolor (sorghum), computational docking studies of homologs of CYP79D1 and CYP71E7 revealed putative interacting surfaces that may facilitate formation of a membrane bound complex [46]. A series of modeling, docking, and membrane association experiments all provided evidence for a three-enzyme complex that, together with downstream enzymes, forms a cyanogenic glucoside metabolon in sorghum.…”

Section: Spatial and Temporal Organization Of Biosynthetic Pathwaysmentioning

confidence: 99%

Harvesting the biosynthetic machineries that cultivate a variety of indispensable plant natural products

Vickery

Clair

Burkart

et al. 2016

Current Opinion in Chemical Biology

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Plants are a sustainable resource for valuable natural chemicals best illustrated by large-scale farming centered on specific products. Here, we review recent discoveries of plant metabolic pathways producing natural products with unconventional biomolecular structures. Prenylation of polyketides by aromatic prenyltransferases (aPTases) ties together two of the major groups of plant specialized chemicals, terpenoids and polyketides, providing a core modification leading to new bioactivities and downstream metabolic processing. Moreover, PTases that biosynthesize Z-terpenoid precursors for small molecules such as lycosantalene have recently been found in the tomato family. Gaps in our understanding of how economically important compounds such as cannabinoids are produced are being identified using next-generation ‘omics’ to rapidly advance biochemical breakthroughs at an unprecedented rate. For instance, olivetolic acid cyclase, a polyketide synthase (PKS) co-factor from Cannabis sativa, directs the proper cyclization of a polyketide intermediate. Elucidations of spatial and temporal arrangements of biosynthetic enzymes into metabolons, such as those used to control the efficient production of natural polymers such as rubber and defensive small molecules such as linamarin and lotaustralin, provide blueprints for engineering streamlined production of plant products.

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“…Based on relative activities detected in microsomes from leaves expressing the native and tagged proteins, eGFP tagging caused 57 and 65% reduction in enzyme activity for CYP73A5 and CYP98A3, respectively (see Supplemental Table 1 online). The presence of the eGFP tag at the C terminus is expected to produce a steric hindrance for P450 interaction with its electron donor CPR, since the C terminus and P450 regions involved in electron transfer (Sevrioukova et al, 1999;Jensen et al, 2011) are located on the same face of the P450 protein. However, the near 40% residual activity of the tagged enzymes indicates that the presence of the eGFP does not completely prevent the P450-CPR interaction.…”

Section: Cyp98a3 and Cyp73a5 Are Mobile With And Within The Ermentioning

confidence: 99%

Protein–Protein and Protein–Membrane Associations in the Lignin Pathway

et al. 2012

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Supramolecular organization of enzymes is proposed to orchestrate metabolic complexity and help channel intermediates in different pathways. Phenylpropanoid metabolism has to direct up to 30% of the carbon fixed by plants to the biosynthesis of lignin precursors. Effective coupling of the enzymes in the pathway thus seems to be required. Subcellular localization, mobility, protein-protein, and protein-membrane interactions of four consecutive enzymes around the main branch point leading to lignin precursors was investigated in leaf tissues of Nicotiana benthamiana and cells of Arabidopsis thaliana. CYP73A5 and CYP98A3, the two Arabidopsis cytochrome P450s (P450s) catalyzing para-and meta-hydroxylations of the phenolic ring of monolignols were found to colocalize in the endoplasmic reticulum (ER) and to form homo-and heteromers. They moved along with the fast remodeling plant ER, but their lateral diffusion on the ER surface was restricted, likely due to association with other ER proteins. The connecting soluble enzyme hydroxycinnamoyltransferase (HCT), was found partially associated with the ER. Both HCT and the 4-coumaroyl-CoA ligase relocalized closer to the membrane upon P450 expression. Fluorescence lifetime imaging microscopy supports P450 colocalization and interaction with the soluble proteins, enhanced by the expression of the partner proteins. Protein relocalization was further enhanced in tissues undergoing wound repair. CYP98A3 was the most effective in driving protein association.

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Homology modeling of the three membrane proteins of the dhurrin metabolon: Catalytic sites, membrane surface association and protein–protein interactions

Cited by 35 publications

References 76 publications

Flowering Plants. Monocots

Flowering Plants. Monocots

Harvesting the biosynthetic machineries that cultivate a variety of indispensable plant natural products

Protein–Protein and Protein–Membrane Associations in the Lignin Pathway

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