حکیم محمد اختر کا فروغ تصوف میں کردار

Sufism is the heart of Islam. It is attached with Islam as the human soul is woven within the body. Sufis have always been the center of Muslim society, especially; in the sub-continent, they have firmly imprinted their marks in every sphere of life. Various mystic traditions as Naqshbandi, Chishti, Qadri etc. Are commonly known in India and Pakistan. This study explores the great Sufi, Hakim Mohammad Akhtar, for his unprecedented services in the field of mystic practices, poetry and Islamic literature. In the initial part of the study, his family background and educational account have been described which show that not only he was a passionate follower of mystic legacy from an early age but a true stalwart of Islam. The historical account of Hakim Akhtar reveals that he was a staunch devotee of Molana Rome which resulted in the form of his famous book "Maarif-e-Masnawi". In the latter part of the study, his character and work are unveiled in a chronological order. As the follower of Sufi tradition, Hakim Akhtar was against personal glorification. Through this research study, some astonishing hidden aspects of his life have been discovered which will help his disciples and devotees to follow the path of their mentor perfectly.

Sequencing and Analysis of a Cdna Encoding a Putative Coclaurine N-Methyltransferase Cnmt from Aristolochia Fimbriata, a Basal Angiosperm

Alkaloids are produced in plants through various pathways involving several enzymes that lead to diverse alkaloids. One of the most important alkaloid biosynthetic enzymes is coclaurine N-methyltransferase (CNMT) which is an S-adenosyl-L- methionine-dependent methyltransferase (SAM-MTase). SAM-MTases utilize S- adenosyl-L-methionine (SAM) as a cofactor to methylate other molecules. CNMT catalyzes the methylation of coclaurine. Crystal structures of more than hundred SAM-MTases have been investigated. Several O-methyltransferases have been characterized at the molecular as well as structural levels, but there have been very few molecular studies of N-methyltransferases especially about CNMTs. In this study, the amino acids sequence of Aristolochia fimbriata putative CNMT has been determined by isolating and translating the full-length cDNA. In order to investigate the mechanism of methylation by this putative CNMT, three-dimensional homology model has been built and the ligand (SAM) as well as the substrate (S- Coclaurine) has been docked into its active site. Phylogenetic analyses were performed using the MEGA 4.0 software. The phylogenetic relationship of A. fimbriata putative CNMT with their homologs has also been analyzed. In order to identify the putative CNMT gene and determine its function, online similarity searches were performed by BLAST program using the cDNA sequence as well as the putative protein that could be encoded by the gene. All the methods, applied, predicted that the gene identified might be involved in the production of CNMT. The predicted homology model consists of two domains: the N-terminal catalytic core domain and the C-terminal domain. The catalytic core domain has a central sheet of β-strands surrounded by α helices. The catalytic core domain contains binding site for VSAM. The C-terminal domain consists of alpha helices and a few beta sheets creating a pocket for the substrate in between them. The SAM-binding pocket is located next to substrate binding pocket and there is an opening in between these two cavities through which the methyl group of SAM projects towards the substrate. The most important residues involved in the methyl transfer reaction seem to be Tyr-79 and Glu-96.