Your browser doesn't support javascript.
loading
[Bioinformatics analysis of geranylgeranyl pyrophosphate synthase coding gene and amino acid sequence in Lamiaceae].
Chen, Yi-Jun; Rong, Qi-Xian; Jiang, Dan; Shen, Ye; Huang, Lu-Qi.
Afiliação
  • Chen YJ; Jiangxi University of Traditional Chinese Medicine, Nanchang 330004, China.
  • Rong QX; State Key Laboratory Breeding Base of Dao-di Herbs, National Resource Center for Chinese Materia Medica, China Academy of Chinese Medical Sciences, Beijng 100700, China.
  • Jiang D; State Key Laboratory Breeding Base of Dao-di Herbs, National Resource Center for Chinese Materia Medica, China Academy of Chinese Medical Sciences, Beijng 100700, China.
  • Shen Y; State Key Laboratory Breeding Base of Dao-di Herbs, National Resource Center for Chinese Materia Medica, China Academy of Chinese Medical Sciences, Beijng 100700, China.
  • Huang LQ; School of Chinese Pharmacy, Beijing University of Chinese Medicine, Beijing 100102, China.
Zhongguo Zhong Yao Za Zhi ; 42(3): 465-472, 2017 Feb.
Article em Zh | MEDLINE | ID: mdl-28952250
ABSTRACT
Geranylgeranyl pyrophosphate synthase enzyme is one of the key enzymes in the synthesis pathway of diterpenoid. Nine Lamiaceae genus GGPS synthase in Genebank was analyzed in this article. GGPS synthase the nucleic acid sequences and amino acid sequences, physicochemical properties, the signal peptide, leader peptides, transmembrane topological structure, hydrophobic, hydrophilic, subcellular localization, secondary structure, function domain, tertiary structure and evolutional relationship were predicted by using bioinformatics methods.Phylogenetic tree was constructed for the geranylgeranyl pyrophosphate synthase enzyme protein family. The results showed that GGPS amino acid sequence of the physical and chemical properties were basically identical, mainly hydrophilic protein, there existed chloroplast transit peptide, and no signal peptide and membrane structure domain, which mainly located in the chloroplast, the minor part located in mitochondria. The main secondary structures of the proteins are alpha helix and random coil. All these proteins have catalytic residues, aspartate-rich region, active site lid residues, substrate-Mg2+ binding site. The results provide theoretical reference for study on both the enzymatic characteristics of GGPS and the biosynthesis pathway of diterpenoid.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Lamiaceae / Geranil-Geranildifosfato Geranil-Geraniltransferase Tipo de estudo: Prognostic_studies Idioma: Zh Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Lamiaceae / Geranil-Geranildifosfato Geranil-Geraniltransferase Tipo de estudo: Prognostic_studies Idioma: Zh Ano de publicação: 2017 Tipo de documento: Article