The Carotenoid Cleavage Dioxygenase 1 Enzyme Has Broad Substrate Specificity, Cleaving Multiple Carotenoids at Two Different Bond Positions

In many organisms, various enzymes mediate site-specific carotenoid cleavage to generate biologically active apocarotenoids. These carotenoid-derived products include provitamin A, hormones, and flavor and fragrance molecules. In plants, the CCD1 enzyme cleaves carotenoids at 9,10 (9′,10′) bonds to...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2008-04, Vol.283 (17), p.11364-11373
Main Authors: Vogel, Jonathan T., Tan, Bao-Cai, McCarty, Donald R., Klee, Harry J.
Format: Article
Language:English
Subjects:
Arabidopsis
Binding Sites
Carotenoids - chemistry
Chromatography, High Pressure Liquid
Cloning, Molecular
Dioxygenases - chemistry
Dioxygenases - physiology
Escherichia coli - metabolism
Gene Expression Regulation, Plant
Lycopene
Lycopersicon esculentum
Models, Biological
Models, Chemical
Plant Proteins - chemistry
Protein Conformation
Substrate Specificity
Zea mays
Zea mays - enzymology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In many organisms, various enzymes mediate site-specific carotenoid cleavage to generate biologically active apocarotenoids. These carotenoid-derived products include provitamin A, hormones, and flavor and fragrance molecules. In plants, the CCD1 enzyme cleaves carotenoids at 9,10 (9′,10′) bonds to generate multiple apocarotenoid products. Here we systematically analyzed volatile apocarotenoids generated by maize CCD1 (ZmCCD1) from multiple carotenoid substrates. ZmCCD1 did not cleave geranylgeranyl diphosphate or phytoene but did cleave other linear and cyclic carotenoids, producing volatiles derived from 9,10 (9′,10′) bond cleavage. Additionally the Arabidopsis, maize, and tomato CCD1 enzymes all cleaved lycopene to generate 6-methyl-5-hepten-2-one. 6-Methyl-5-hepten-2-one, an important flavor volatile in tomato, was produced by cleavage of the 5,6 or 5′,6′ bond positions of lycopene but not geranylgeranyl diphosphate, ζ-carotene, or phytoene. In vitro, ZmCCD1 cleaved linear and cyclic carotenoids with equal efficiency. Based on the pattern of apocarotenoid volatiles produced, we propose that CCD1 recognizes its cleavage site based on the saturation status between carbons 7 and 8 (7′ and 8′) and carbons 11 and 12 (11′ and 12′) as well as the methyl groups on carbons 5, 9, and 13 (5′, 9′, and 13′).
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M710106200