Metabolons involving plant cytochrome P450s

被引：81

作者：

Ralston L. ^{[1
]}

Yu O. ^{[2
]}

机构：

[1] Sigma-Aldrich Biotechnology, Life Science and High Technology Center, St. Louis, MO 63103

[2] Donald Danforth Plant Science Center, St. Louis, MO 63132

来源：

Phytochemistry Reviews | 2006年 / 5卷 / 2-3期

基金：

美国国家科学基金会;

关键词：

Cytochrome P450; Cytochrome P450 reductase; Enzyme interaction; ER localization; Metabolon;

D O I：

10.1007/s11101-006-9014-4

中图分类号：

学科分类号：

摘要：

Arranging biological processes into "compartments" is a key feature of all eukaryotic cells. Through this mechanism, cells can drastically increase metabolic efficiency and manage complex cellular processes more efficiently, saving space and energy. Compartmentation at the molecular level is mediated by metabolons. A metabolon is an ordered protein complex of sequential metabolic enzymes and associated cellular structural elements. The sub-cellular organization of enzymes involved in the synthesis and storage of plant natural products appears to involve the anchoring of metabolons by cytochrome P450 monooxygenases (P450s) to specific domains of the endoplasmic reticulum (ER) membrane. This review focuses on the current evidence supporting the organization of metabolons around P450s on the surface of the ER. We outline direct and indirect experimental data that describes P450 enzymes in the phenylpropanoid, flavonoid, cyanogenic glucoside, and other biosynthetic pathways. We also discuss the limitations and future directions of metabolon research and the potential for application to metabolic engineering endeavors. © 2006 Springer Science+Business Media B.V.

引用

页码：459 / 472

页数：13

共 90 条

[1]

Achnine L., Blancaflor E.B., Rasmussen S., Dixon R.A., Colocalization of L-phenylalanine ammonialyase and cinnamate 4-hydroxylase for metabolic channeling in phenylpropanoid biosynthesis, Plant Cell, 16, pp. 3098-3109, (2004)

[2]

Akashi T., Sawada Y., Aoki T., Ayabe S., New scheme of the biosynthesis of formononetin involving 2,7,4′-trihydroxyisoflavanone but not daidzein as the methyl acceptor, Biosci Biotechnol Biochem, 64, pp. 2276-2279, (2000)

[3]

Akashi T., Sawada Y., Shimada N., Sakurai N., Aoki T., Ayabe S., cDNA cloning and biochemical characterization of S-adenosyl-L-methionine: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase, a critical enzyme of the legume isoflavonoid phytoalexin pathway, Plant Cell Physiol, 44, pp. 103-112, (2003)

[4]

Anderson K.S., Kim A.Y., Quillen J.M., Sayers E., Yang X.J., Miles E.W., Kinetic characterization of channel impaired mutants of tryptophan synthase, J Biol Chem, 270, (1995)

[5]

Bak S., Olsen C.E., Petersen B.L., Moller B.L., Halkier B.A., Metabolic engineering of p-hydroxybenzylglucosinolate in Arabidopsis by expression of the cyanogenic CYP79A1 from Sorghum bicolor, Plant J, 20, pp. 663-671, (1999)

[6]

Bayburt T.H., Carlson J.W., Sligar S.G., Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer, J Struct Biol, 123, pp. 37-44, (1998)

[7]

Bayburt T.H., Sligar S.G., Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks, Proc Natl Acad Sci USA, 99, pp. 6725-6730, (2002)

[8]

Blancaflor E.B., Gilroy S., Plant cell biology in the new millennium: New tools and new insights, Am J Bot, 87, pp. 1547-1560, (2000)

[9]

Blount J.W., Korth K.L., Masoud S.A., Rasmussen S., Lamb C., Dixon R.A., Altering expression of cinnamic acid 4-hydroxylase in transgenic plants provides evidence for a feedback loop at the entry point into the phenylpropanoid pathway, Plant Physiol, 122, pp. 107-116, (2000)

[10]

Boudet A.M., Kajita S., Grima-Pettenati J., Goffner D., Lignins and lignocellulosics: A better control of synthesis for new and improved uses, Trends Plant Sci, 8, pp. 576-581, (2003)

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