Bioinformation analysis of chorismate synthase in Baphicacantus cusia and other 78 species of plants.
10.19540/j.cnki.cjcmm.20180105.002
- Author:
Jian YU
1
;
Qi YE
1
;
Shu-Ju NING
2
;
Qing LI
3
;
He-Xin TAN
4
;
Jing-Xian FENG
3
;
Rui-Bing CHEN
4
;
Xiao-Li MA
1
;
Pei-Min GONG
1
;
Xuan-Xuan ZHAO
1
;
Lei ZHANG
4
;
Dao-Zhi WEI
1
Author Information
1. College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
2. College of Crop Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
3. Changzheng Hospital, Second Military Medical University, Shanghai 200003, China.
4. Department of Pharmaceutical Botany, School of Pharmacy, Second Military Medical University, Shanghai 200433, China.
- Publication Type:Journal Article
- Keywords:
Baphicacanthus cusia;
bioinformatics;
chorismate synthase;
structure modification;
structure-activity relationship
- MeSH:
Acanthaceae;
enzymology;
Amino Acid Sequence;
Computational Biology;
Phosphorus-Oxygen Lyases;
chemistry;
Phylogeny;
Plant Proteins;
chemistry;
Protein Structure, Secondary
- From:
China Journal of Chinese Materia Medica
2018;43(4):721-730
- CountryChina
- Language:Chinese
-
Abstract:
Chorismate synthase(CS, EC:4.2.3.5) catalyses 5-enolpyruvy-shikimate-3-phosphate to form chorismate, which is the essential enzyme for chorismate biosynthesis in organisms. The amino acid sequences of CS from 79 species of higher plants were reported in GenBank at present. 125 amino acid sequences of CS from Baphicacanthus cusia and other 78 species of plants were predicted and analyzed by using various bioinformatics software, including the composition of amino acid sequences, signal peptide, leader peptide, hydrophobic/hydrophilic, transmembrane structure, coiled-coil domain, protein secondary structure, tertiary structure and functional domains. The phylogenetic tree of CS protein family was constructed and divided into eight groups by phylogenetic analysis. The homology comparison indicated that B. cusia shared a high homology with several plants such as Sesamum indicum, Nicotiana tabacum, Solanum tuberosum and so on. The open reading frame(ORF) of all samples is about 1 300 bp, the molecular weight is about 50 kDa, the isoelectric point(pI) is 5.0-8.0 which illustrated that CS protein is slightly basic. The ORF of CS we cloned in B. cusia is 1 326 bp, the amino acid residues are 442, the molecular weight is 47 kDa and pI is 8.11. The CS in B.cusia showed obvious hydrophobicity area and hydrophilicity area, no signal peptide, and may exists transmembrane structure areas. The main secondary structures of CS protein are random coil and Alpha helix, also contain three main structural domains which are an active structural domain, a PLN02754 conserved domain and a FMN binding site. The acquired information in this study would provide certain scientific basis for further study on structure-activity relationship and structure modification of CS in plants in the future.
