In an enzyme-catalyzed reaction, the substrate must first attachÃ© to the enzyme. The substrate is relatively smaller than the enzyme. Therefore, the substrate is binding with a portion of the enzyme. The substrate is attached to the enzyme with weak bonding forces such as hydrogen bond, electrostatic interactions, and dipole-dipole interactions. The substrates are usually complementary to the enzymes. However, it is possible that they do not fit perfectly each other. These bonding forces help the complex to be more stable. In the case of two substrate reactions involving ternary complex, two substrates must be bound close to each other to precede the reaction. It is impossible to proceed the reaction if two substrates are not adjacent or close each other spatially. From the case, the enzyme should have some steric specificity. OMICS Group International is one of the leading Open Access Publishers which is publishing 700+ peer-reviewed journals with the dramatic effort of editorial board members. OMICS Group through its Open Access Initiative is committed to make genuine and reliable contributions to the scientific community. It follows an Open Access publication model that enables the dissemination of research articles to the global community free of cost. Journal of Glycobiology publishes original research articles, novel, and scientifically sound findings dealing with Cancer Glycobiology, Glycopeptides, drug discovery and Glycomics, Fucanomes and Galactanomes, Structural Glycobiology, Membrane glycoproteins, Protein De glycosylation and carbohydrate diet. Journal of Glycobiology is among the top Scholarly open access journals which publishes the articles related to Substrate Specificity . Journal of Glycobiology provide a forum for Scientists from all over the world to exchange ideas, to propagate the advancement of science.
Last date updated on June, 2014