Phytochemistry Reviews

, 5:459

Metabolons involving plant cytochrome P450s

Original Paper

DOI: 10.1007/s11101-006-9014-4

Cite this article as:
Ralston, L. & Yu, O. Phytochem Rev (2006) 5: 459. doi:10.1007/s11101-006-9014-4

Abstract

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.

Keywords

Cytochrome P450 Metabolon Enzyme interaction ER localization Cytochrome P450 reductase 

Abbreviations

4CL

4-Coumarate: CoA ligase

AFM

Atomic force microscopy

C4H

Cinnamate 4-hydroxylase

CHI

Chalcone isomerase

CHS

Chalcone synthase

CPR

NADPH-cytochrome P450 reductase

DFR

Dihydroflavonol reductase

ER

Endoplasmic reticulum

F3H

Flavanone 3β-hydroxylase

F3′H

Flavonoid 3′-hydroxylase

F3′5′H

Flavonoid 3′,5′-hydroxylase

FLIM

Fluorescence lifetime imaging microscopy

FRET

Fluorescence energy resonance transfer

I2′H

Isoflavone 2′-hydroxylase

IFS

Isoflavone synthase

IOMT

Isoflavone O-methyltransferase

P450

Cytochrome P450 monooxygenase

PAL

Phenylalanine ammonia-lyase

Copyright information

© Springer Science+Business Media B.V. 2006

Authors and Affiliations

  1. 1.Sigma-Aldrich BiotechnologyLife Science and High Technology CenterSt. LouisUSA
  2. 2.Donald Danforth Plant Science CenterSt. LouisUSA

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