Studies in alkaloid biosynthesis

Imperial Users onl

Leadership-The Most Important Area of Educational Performance

Leadership is seen as the most critical aspect in successfully developing educational institutions, supporting stated aims and objectives, and enhancing education. It is a vital aspect in determining whether an organization succeeds or fails. A leader's style is defined by how he guides and encourages others to accomplish institutional objectives. Basic skills are described as "a collection of psychological and social areas of expertise and interpersonal skills that enable individuals to make informed choices, resolve issues, think critically and analytically, effectively communicate, develop relationships, empathize with others, and cope and enhance their quality of life, productively and healthily." This research aims to determine the effect of Leadership as a practical skill on educational establishments. From the perspective of the school, the principal's Leadership is critical. His function and responsibilities will impact all facets of the school organization’s life. At the executive level of the school, the principal's Leadership is the significant variable that serves as a bridge between individual lives and the future outlook of any institution. This research aims to demonstrate how Leadership as a practical skill, affects educational institution’s performance. This is a conceptual study that provides a theoretical foundation for the notion. The reports and findings indicate that leadership style plays a critical role in boosting an institution's success since it influences the organization's culture and the value of its personnel

AN AYURVEDIC MANAGEMENT OF EKAKUSHTHA (PSORIASIS VULGARIS) THROUGH VIRECHANA KARMA (PURGATION THERAPY) AND SHAMANA CHIKITSA (PALLIATIVE THERAPY): A CASE STUDY

A 21 years old female patient had complained of silvery scaly skin lesions all over body with reddish discoloration having severe itching, burning sensation since 15 years back that got aggravated during each rainy and cold season. Examination- 1. Severe silvery scaly lesions shaded down on rubbing all over the day, 2. Characterized by sharply demarcated and erythematous papulosquamous lesions (Dry, thin, silvery-white scales), 3. Irregular, discoid and oval in shape. 3. Small areas of bleeding where the involved skin is scratched, 4. Scaly plaques on the scalp, 5. Auspitz Sign-positive, 6. Candle grease sign-Positive, 7. Grattage Test-Positive. Aims and Objectives: To prove the role & efficacy of Virechana drugs, Virechana Karma, Sansarjana Karma & Sanshamana chikitsa. Materials and Methods: 1. Dadimashtaka Choorna was given 5gm twice a day with lukewarm water continuously for 3 days as Aama Dosha Pachanartha, 2.Guggulutiktakaghritama was given 25ml, 50ml, 75ml, 100ml, 125ml, 150ml & 200ml with lukewarm water for next 7 days as Snehana Karma, 3. Bahya Snehana with Dashamoola Taila and Bahya Sarvaanga Swedana with Dashmoola Kwatha were applied for next 3 days, 4.Virechana Karma was done after Samyaka Snehana & Swedana. 5. Sansarjana Karma was done after Samayaka Virechana for 7 days. Differential Diagosis-Sidddham, Mandalkushtha & Ekakushtha. Provisional Dignosis-Ekakushtha, Final Diagnosis-Ekakushtha (Psoriasis vulgaris). Result: Significantly improvements were observed in treatment of Ekakushtha (Psoriasis vulgaris). Discussion: Deepana & Pachana chikitsa is responsible for Aama Dosha Pachanartha. Snehana is responsible for Srotosamamardawama. Swedana is responsible for Srotomargavishodhanam. Virechana is responsible for pacifying vitiated Pittaja as well as Kaphaja Dosha and Vyadhi

Cation induced differential effect on structural and functional properties of Mycobacterium tuberculosis α-Isopropylmalate synthase

<p>Abstract</p> <p>Background</p> <p>α-isopropylmalate synthase (MtαIPMS), an enzyme that catalyzes the first committed step of the leucine biosynthetic pathway of <it>Mycobacterium tuberculosis </it>is a potential drug target for the anti-tuberculosis drugs. Cations induce differential effect of activation and inhibition of MtαIPMS. To date no concrete mechanism for such an opposite effect of similarly charged cations on the functional activity of enzyme has been presented.</p> <p>Results</p> <p>Effect of cations on the structure and function of the MtαIPMS has been studied in detail. The studies for the first time demonstrate that different cations interact specifically at different sites in the enzyme and modulate the enzyme structure differentially. The inhibitors Zn²⁺and Cd²⁺ions interact directly with the catalytic domain of the enzyme and induce unfolding/denaturation of the domain. The activator K⁺also interacts with the catalytic TIM barrel domain however, it does not induce any significant effect on the enzyme structure. Studies with isolated catalytic TIM barrel domain showed that it can carry out the catalytic function on its own but probably requires the non-catalytic C-terminal domain for optimum functioning. An important observation was that divalent cations induce significant interaction between the regulatory and the catalytic domain of MtαIPMS thus inducing structural cooperativity in the enzyme. This divalent cation induced structural cooperativity might result in modulation of activity of the catalytic domain by regulatory domain.</p> <p>Conclusion</p> <p>The studies for the first time demonstrate that different cations bind at different sites in the enzyme leading to their differential effects on the structure and functional activity of the enzyme.</p

Guanidine hydrochloride- and urea-induced unfolding of Toxoplasma gondii ferredoxin-NADP<SUP>+</SUP> reductase: stabilization of a functionally inactive holo-intermediate

Usually during the folding/unfolding of flavoproteins, an apo-intermediate is stabilized before global unfolding of the enzymes occurs. However, stabilization of a holo-intermediate has also been reported for a few flavoproteins. We have studied the unfolding of Toxoplasma gondii ferredoxin-NADP+ reductase (TgFNR) using GdnHCl and urea. A functionally inactive holo-intermediate of the enzyme was found to be stabilized during this unfolding process. The intermediate species had cofactor FAD bound to it, but it showed free movement due to which the stabilized intermediates were functionally inactive. The native TgFNR behaves cooperatively with the two structural domains interacting strongly with each other. The denaturants GdnHCl and urea, at low concentrations, were found to interact selectively with the NADP+-binding domain of TgFNR and to induce structural modifications in it. These selective modifications in the protein molecule lead to loss of interactions between two domains and the enzyme behaved non-cooperatively resulting in stabilization of an intermediate species. Significant differences in the structural properties of the GdnHCl- and urea-stabilized holo-intermediates of TgFNR were observed. Comparison of the unfolding pathway of TgFNR (a plant-type FNR) with that of FprA (a GR-type FNR) demonstrates that they follow very different pathways of unfolding

Unusual structural, functional, and stability properties of serine hydroxymethyltransferase from Mycobacterium tuberculosis

From the genome analysis of the Mycobacterium tuberculosis two putative genes namely GlyA and GlyA2 have been proposed to encode for the enzyme serine hydroxymethyltransferase. We have cloned, overexpressed, and purified to homogeneity their respective protein products, serine hydroxymethyltransferase, SHM1 and SHM2. The recombinant SHM1 and SHM2 exist as homodimers of molecular mass about 90 kDa under physiological conditions, however, SHM2 has more compact conformation and higher thermal stability than SHM1. The most interesting structural observation was that the SHM1 contains 1 mol of pyridoxal 5&#8242;-phosphate (PLP)/mol of enzyme dimer. This is the first report of such a unique stoichiometry of PLP and enzyme dimer for SHMT. The SHM2 contains 2 mol of PLP/mol of enzyme dimer, which is the usual stoichiometry reported for SHMT. Functionally both the recombinant enzymes showed catalysis of reversible interconversion of serine and glycine and aldol cleavage of a 3-hydroxyamino acid. However, unlike SHMT from other sources both SHM1 and SHM2 do not undergo half-transamination reaction with d-alanine resulting in formation of apoenzyme but l-cysteine removed the prosthetic group, PLP, from both the recombinant enzymes leaving the respective inactive apoenzymes. Comparative structural studies on the two enzymes showed that the SHM1 is resistant to alkaline denaturation up to pH 10.5, whereas the native SHM2 dimer dissociates into monomer at pH 9. urea- and guanidinium chloride-induced two-step unfolding of SHM1 and SHM2 with the first step being dissociation of dimer into apomonomer at low denaturant concentrations followed by unfolding of the stabilized monomer at higher denaturant concentrations