Identification of neoxanthin synthase as a carotenoid cyclase paralog

Citation
F. Bouvier et al., Identification of neoxanthin synthase as a carotenoid cyclase paralog, EUR J BIOCH, 267(21), 2000, pp. 6346-6352
Citations number
44
Categorie Soggetti
Biochemistry & Biophysics
Journal title
EUROPEAN JOURNAL OF BIOCHEMISTRY
ISSN journal
00142956 → ACNP
Volume
267
Issue
21
Year of publication
2000
Pages
6346 - 6352
Database
ISI
SICI code
0014-2956(200011)267:21<6346:IONSAA>2.0.ZU;2-L
Abstract
Neoxanthin, a precursor of the plant hormone abscisic acid, is an allenic x anthophyll recognized as the last product of carotenoid synthesis in green plants. A cDNA for neoxanthin synthase (NSY) was isolated from tomato using a molecular approach based on the mechanistic and structural similarities of NSY to two other closely related carotenogenic enzymes, lycopene cyclase (LCY) and capsanthin-capsorubin synthase (CCS). The identified tomato NSY cDNA (T.NSY) encodes a 56-kDa plastid-targeted protein that when expressed in Escherichia coli, catalyzes the conversion of violaxanthin to neoxanthin . In tobacco leaves that transiently express T.NSY, an increase in neoxanth in content with a concomitant decrease in violaxanthin is observed. NSY is structurally similar to LCY and CCS. However, in Cyanobacteria, the general ly accepted progenitor of plastids, both CCS and NSY are absent while LCY i s present. LCY catalyzes a simplified version of the reaction catalyzed by NSY and CCS suggesting that these two enzymes were remodeled from LCY durin g higher plant evolution to create new forms of oxidized carotenoids.