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Corresponding Enzyme (corresponding + enzyme)
Selected AbstractsThe crystal structure of pyruvate decarboxylase from Kluyveromyces lactisFEBS JOURNAL, Issue 18 2006Implications for the substrate activation mechanism of this enzyme The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis has been determined to 2.26 Å resolution. Like other yeast enzymes, Kluyveromyces lactis pyruvate decarboxylase is subject to allosteric substrate activation. Binding of substrate at a regulatory site induces catalytic activity. This process is accompanied by conformational changes and subunit rearrangements. In the nonactivated form of the corresponding enzyme from Saccharomyces cerevisiae, all active sites are solvent accessible due to the high flexibility of loop regions 106,113 and 292,301. The binding of the activator pyruvamide arrests these loops. Consequently, two of four active sites become closed. In Kluyveromyces lactis pyruvate decarboxylase, this half-side closed tetramer is present even without any activator. However, one of the loops (residues 105,113), which are flexible in nonactivated Saccharomyces cerevisiae pyruvate decarboxylase, remains flexible. Even though the tetramer assemblies of both enzyme species are different in the absence of activating agents, their substrate activation kinetics are similar. This implies an equilibrium between the open and the half-side closed state of yeast pyruvate decarboxylase tetramers. The completely open enzyme state is favoured for Saccharomyces cerevisiae pyruvate decarboxylase, whereas the half-side closed form is predominant for Kluyveromyces lactis pyruvate decarboxylase. Consequently, the structuring of the flexible loop region 105,113 seems to be the crucial step during the substrate activation process of Kluyveromyces lactis pyruvate decarboxylase. [source] Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2ACTA CRYSTALLOGRAPHICA SECTION D, Issue 12 2003Eugenia Pechkova The three-dimensional crystal structure of the triple-point mutant of the catalytic subunit of human protein kinase CK2, has been determined at 2.4,Å resolution. Microcrystals of mutant CK2 catalytic subunit were obtained by a protein-crystallization method based on thin-film nanotechnology. These microcrystals (of about 20,µm in diameter) were used for diffraction data collection by means of the microfocus beamline at the ESRF synchrotron. A comparison between the human protein kinase CK2, and the corresponding enzyme from a lower organism (Zea mays) is made. [source] Assessment of Growth, Physiological and Biochemical Parameters and Activities of Antioxidative Enzymes in Salinity Tolerant and Sensitive Basmati Rice VarietiesJOURNAL OF AGRONOMY AND CROP SCIENCE, Issue 6 2007M. P. Singh Abstract This investigation was undertaken to compare the level of salinity tolerance of the newly bred CSR-30 basmati rice variety with that of the salinity sensitive HBC-19 and Pokkali rice varieties. Twenty-one-day-old hydroponically raised seedlings at 6 and 12 dS m,1 were investigated for growth, photosynthetic rate, chlorophyll content, ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) activity, relative water content (RWC), membrane stability index (MSI), lipid peroxidation, Na/K ratio and activities and gene expression of various isoforms of antioxidative enzymes. Salinity stress led to reduction in shoot length, leaf area, dry weight, RWC, MSI, rate of photosynthesis, chlorophyll content and Rubisco activity in all the three rice varieties. The levels of reduction in these parameters were maximal in HBC-19 followed by those in CSR-30 and Pokkali respectively. Cumulative superoxide dismutase (SOD) activity increased in Pokkali and CSR-30 in consonance with increase in salinity stress while it decreased in HBC-19. The Mn-SOD activity however, was enhanced in all three varieties in the presence of salinity stress while the activities of Fe-SOD, Cu/Zn-SOD and ascorbate peroxidase were decreased in HBC-19 when compared with CSR-30 and Pokkali. The activity of catalase (CAT) was higher in HBC-19 when compared with its activity in CSR-30 and Pokkali. The levels of gene expressions of the three isoforms of SOD ascertained by reverse transcriptase polymerase chain reaction were not necessarily indicative of the activities of the corresponding enzymes. Thus, despite the maximal enhancement in gene expression of Fe-SOD in HBC-19 in response to salinity stress, the activity of this enzyme in HBC-19 remained low. Similarly, despite a marginal increase in gene expression of Cu-Zn SOD in the three varieties, its activity was significantly higher in Pokkali and CSR-30 when compared with that in HBC-19. A significant enhancement in the activity of CAT at 12 dS m,1 in HBC-19 when compared with CSR-30 and Pokkali might confer a degree of tolerance to H2O2 stress in this variety in the presence of higher levels of NaCl at the seedling stage. [source] On the Generation of Catalytic Antibodies by Transition State AnaloguesCHEMBIOCHEM, Issue 4 2003Montserrat Barbany Abstract The effective design of catalytic antibodies represents a major conceptual and practical challenge. It is implicitly assumed that a proper transition state analogue (TSA) can elicit a catalytic antibody (CA) that will catalyze the given reaction in a similar way to an enzyme that would evolve (or was evolved) to catalyze this reaction. However, in most cases it was found that the TSA used produced CAs with relatively low rate enhancement as compared to the corresponding enzymes, when these exist. The present work explores the origin of this problem, by developing two approaches that examine the similarity of the TSA and the corresponding transition state (TS). These analyses are used to assess the proficiency of the CA generated by the given TSA. Both approaches focus on electrostatic effects that have been found to play a major role in enzymatic reactions. The first method uses molecular interaction potentials to look for the similarity between the TSA and the TS and, in principle, to help in designing new haptens by using 3D quantitative struture,activity relationships. The second and more quantitative approach generates a grid of Langevin dipoles, which are polarized by the TSA, and then uses the grid to bind the TS. Comparison of the resulting binding energy with the binding energy of the TS to the grid that was polarized by the TS provides an estimate of the proficiency of the given CA. Our methods are used in examining the origin of the difference between the catalytic power of the 1F7 CA and chorismate mutase. It is demonstrated that the relatively small changes in charge and structure between the TS and TSA are sufficient to account for the difference in proficiency between the CA and the enzyme. Apparently the environment that was preorganized to stabilize the TSA charge distribution does not provide a sufficient stabilization to the TS. The general implications of our findings and the difficulties in designing a perfect TSA are discussed. Finally, the possible use of our approach in screening for an optimal TSA is pointed out. [source] |