Genomewide Analysis of Carotenoid Cleavage Dioxygenases in Unicellular and Filamentous Cyanobacteria

被引：31

作者：

Cui, Hongli ^{[1
,2
]}

Wang, Yinchu ^{[1
,2
]}

Qin, Song ^{[1
]}

机构：

[1] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Coastal Zonebio Resource Lab, Yantai 264003, Peoples R China

[2] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Grad Univ, Beijing 100049, Peoples R China

来源：

COMPARATIVE AND FUNCTIONAL GENOMICS | 2012年

基金：

中国国家自然科学基金;

关键词：

IN-VITRO CHARACTERIZATION; NOSTOC SP PCC-7120; ABSCISIC-ACID; SWISS-MODEL; BIOCHEMICAL-CHARACTERIZATION; SUBSTRATE-SPECIFICITY; RETINAL BIOSYNTHESIS; OXIDATIVE CLEAVAGE; CROCUS-SATIVUS; YELLOW PIGMENT;

D O I：

10.1155/2012/164690

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Carotenoid cleavage dioxygenases (CCDs) are a group of enzymes that catalyze the oxidative cleavage steps from carotenoids to various carotenoid cleavage products. Some ccd genes have been identified and encoded enzymes functionally characterized in many higher plants, but little in cyanobacteria. We performed a comparative analysis of ccd sequences and explored their distribution, classification, phylogeny, evolution, and structure among 37 cyanobacteria. Totally 61 putative ccd sequences were identified, which are abundant in Acaryochloris marina MBIC 11017, filamentous N-2-fixing cyanobacteria, and unicellular cyanobacterial Cyanothece. According to phylogenetic trees of 16S rDNA and CCD, nced and ccd8 genes occur later than the divergence of ccd7, apco, and ccd1. All CCD enzymes share conserved basic structure domains constituted by a single loop formed with seven beta-strands and one helix. In this paper, a general framework of sequence-function-evolution connection for the ccd has been revealed, which may provide new insight for functional investigation.

引用

页数：13