Sulayman Bin Musa Al-Kala As Sirah Writer an Introduction and Research Analysis

Abu Al-Rab฀ ‘ Sulaym฀n Bin M฀sá Al-Kal฀‘฀ (565 A. H -- 634 A. H) is a great S฀rah writer. In this article, his scholarly and personal characteristics, the list of his works, tributes from scholars to his services and scholarly rank of Al-Kal฀‘฀ are presented. After presenting his personal features, an introduction and research analysis of his book “AlIktif฀’ fi Magh฀z฀ Al-Mu฀tafá wa Al-thal฀thah Al-Khulaf฀ ’ ” is given. Al-Kal฀‘฀ was a great scholar and authentic S฀rah writer. He got knowledge of Had฀th from Abul ‘At฀’. He attended the lectures of various scholars of Had฀th such as Abul Q฀sim bin Al-Jaysh, Abu Bakr bin Jadd, Abu Abdull฀h bin Zark฀n, Abdull฀h bin Fakhkh฀r, Abu Muhammad bin Jamh฀r, Najbah bin Yahy฀. Many great scholars of Had฀th such as Q฀฀฀ T฀nas were his pupils and brought his knowledge to far off countries. Al-Kal฀‘฀ wrote many books on Had฀th and S฀rah. Ibn Farh฀n, Abul Abb฀s and many other scholars have praised and paid tribute to Al-Kal฀‘฀ in their works. Main objective of the book under discussion, Al-Iktif฀’, is to disseminate knowledge of S฀rah and Had฀th prolifically. Al-Kal฀‘฀ has kept in mind the caution and the principles of S฀rah writing derived from the Holy Qur’฀n. Sulaym฀n Bin M฀sá has a great quality of writing S฀rah books. He can be called a born scholar and a writer. His quest for knowledge took him in different cities and he gained the best of knowledge and intellect that can be seen in all of his writings. He can be called a preserver and a protector of S฀rah literature. He is considered the most honored and dignified person among the scientific and cultural tradition of Andalusiyah. This article proves his abilities, qualities and excellence of work.

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.