Bioinformatics analysis of copalyl diphosphate synthase in Salviae Miltiorrhizae Radix et Rhizoma
10.7501/j.issn.0253-2670.2015.06.020
- Author:
Qing LI
1
Author Information
1. Department of Pharmacy, Shanghai Changzheng Hospital, Second Military Medical University
- Publication Type:Journal Article
- Keywords:
Bioinformatics;
Copalyl diphosphate synthase;
Primary structure;
Salviae Miltiorrhizae Radix et Rhizoma;
Secondary structure;
Tertiary structure
- From:
Chinese Traditional and Herbal Drugs
2015;46(6):887-894
- CountryChina
- Language:Chinese
-
Abstract:
To provide the useful information for the further study of copalyl diphosphate synthase (CPS) of Salviae Miltiorrhizae Radix et Rhizoma through amino acid (aa) sequences comparison in S. miltiorrhiza and other plants. Bioinformatics analysis methods were used to perform the prediction of composition and physicochemical character, leader peptide, signal peptide, transmembrane domain, hydrophobicity/hydrophilicity, secondary structure, tertiary structure, and functional domain of 18 CPS amino acid sequences in S. miltiorrhiza and other different plants which belong to 16 species and 13 families. Homology analysis and phylogenetic trees of CPS were also carried out. Most CPS proteins contain more than 730 aa. Their molecular weight is approximately 91 610 and the isoelectric point of them is about 5.87, which suggests that CPS is acidic protein. The results of the sequence structure prediction show that CPS has apparent hydrophobic region and hydrophilicity region, no signal peptide, no transmembrane domain, and may probably have chloroplast transit peptide. The main secondary structures of the proteins are α-helix and random coil. Homology analysis reveals that S. miltiorrhiza has the highest homology comparied with Rosmarinus officinalis and Scoparia dulcis. This work provides a systemic sequence analysis of CPS in S. miltiorrhiza and other plants. It will provide the useful information for CPS studies in the future.
