Author:
Basyuni M,Hayati R,Sihaloho M A,Slamet B,Bimantara Y,Habsyah T S,Hanafiah D S,Julianti E
Abstract
Abstract
Durio zibethinus Murr. (Malvaceae) is well known to produce secondary metabolites and has been described to contain several biological activities. The present study reports the bioinformatics approach to determine ten probably polyprenol reductase from durian (Durio zibethinus Murr.). The length of the gene was varied from 1313 to 1702 bp with protein length from 317 to 412 amino acid. Several physicochemical parameters of polyprenol reductase in D. zibethinus were varied among the genes observed. Based on stability coefficients, ten D. zibethinus genes were unstable proteins except for X5 variant. The genes were mostly stored in the plasma membrane, chloroplast thylakoid membrane, Golgi body, and endoplasmic reticulum (membrane). In contrast to this observation, a few genes existed to the microbody (peroxisome), mitochondrial inner membrane, and endoplasmic reticulum (lumen). To clarify the homology in the group of the polyprenol reductase gene in D. zibethinus, a dendrogram tree was constructed. A clustering showed that polyprenol reductase in D. zibethinus consisted of three branches. The present results indicated the prominence of understanding the disparity and function of physical and chemical features of the different amino acids in plant polyprenol reductase genes in D. zibethinus.
Cited by
3 articles.
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