This observation rules out the involvement of fructosyl nucleotide in its biosynthesis if it is assumed that fructose- 2-phosphate is the necessary component for the biosynthesis of nucleoside diphosphate fructose.
Giving Schmidt We are using biochemical, cell biological, genetic, and molecular approaches in conjunction with the yeast system to better understand the function of enzymes involved in the production of isoprenylated proteins. Examples of isoprenylated proteins include the Ras family of oncoproteins, Ras-related proteins, kinases, and secreted fungal mating pheromones, among many others.
Understanding the function of these proteases may lead to novel therapeutic strategies for cancer, Alzheimer's disease, and other diseases. The farnesyl transferase FTase acts on proteins with a CaaX motif such that the Cysteine of the motif becomes covalently modified with the farnesyl lipid.
The specificity of the FTase is being investigated using both in vivo and in vitro reporters. We are specifically testing whether the FTase has broader specificity than previously proposed.
Rce1p and Ste24p are ER membrane-localized proteases.
These proteases are essential for the maturation of isoprenylated molecules that are involved in a variety of cellular processes. Because Rce1p is specifically required for maturation of the oncoproteins Ras and RhoB, we are aiming to define the proteolytic mechanism of Rce1p and to develop pharmacological inhibitors that have anti-tumor potential.
Rce1p has partial overlapping function with the ER membrane-localized, zinc-dependent Ste24p protease, which has been linked to premature aging progeria because of its role in the processing of lamin A. Thus, we are also trying to understand the functional differences of Rce1p and Ste24p to better understand their relative physiological importance.
These zinc-dependent enzymes are evolutionarily widespread from bacteria to humans. Examples include Ste23p and Axl1p, which mediate production of the yeast a-factor mating pheromone, and the insulin-degrading enzyme, which has a proposed protective function in Alzheimer's disease AD.
Our research on is designed is to gain a better understanding of these largely uncharacterized proteases, thus potentially providing novel insight into new methods for the treatment of AD.producing FOS from FTase had captured much attention from industrial level due to mass production and controlled environment rather than FOS produced from plant.
Many researchers produced crude FTase enzyme to produce FOS. In view of that, purification of crude enzyme from microfungi is studied in order to obtain high yield of FOS.
Fructosyl transferase was found to be distributed both in the extracellular fraction as well as in the intracellular fraction. Among the strains screened, Aureobasidium pullulans, Aspergillus oryzae and Aspergillus flavus were found to possess high titres of FTase activity in that order resulting in higher yields of FOS.
In this report we describe the purification, () De novo synthesis of fructans from sucrose in vitro by a combination of two purified enzymes (sucrose sucrose 1-fructosyl transferase and fructan fructan 1-fructosyl transferase) from chicory roots (Cichorium intybus L.).
A comparison of the in vitro properties of fructosyl transferase activities with the characteristics of in vivo fructan accumulation * Authors. A. J. CAIRNS, 8 WIM ENDE, ANDRÉ LAERE, Purification and properties of an invertase with sucrose: sucrose fructosyltransferase (SST) activity from the roots of Cichorium intybus L.
Purification and characterization of the enzymes of fructan biosynthesis in tubers of Helianthus tuberosus 'Colombia'. 1. Fructan: fructan fructosyl transferase.
FTase catalyzes the transfer of the farnesyl group from farnesyl diphosphate to proteins containing a C-terminal CaaX motif, where 'C' is a conserved cysteine that is the site of farnesyl modification, 'a' is usually an aliphatic amino acid, and 'X' is methionine, serine, glutamine, or alanine.