A5035833525- Drug Transport and Resistance Mechanisms
- Peptidase Inhibition and Analysis
- Cancer Research and Treatments
- Enzyme Structure and Function
- Tuberculosis Research and Epidemiology
- Macrophage Migration Inhibitory Factor
- Metabolism and Genetic Disorders
- Salmonella and Campylobacter epidemiology
- Steroid Chemistry and Biochemistry
- Appendicitis Diagnosis and Management
- Peroxisome Proliferator-Activated Receptors
- Synthesis and Reactions of Organic Compounds
- Mycobacterium research and diagnosis
- Receptor Mechanisms and Signaling
- Synthesis and Biological Evaluation
- Hernia repair and management
- Biochemical and Molecular Research
- Arsenic contamination and mitigation
- bioluminescence and chemiluminescence research
- Metal complexes synthesis and properties
- Signaling Pathways in Disease
- Nitrogen and Sulfur Effects on Brassica
- Pharmacogenetics and Drug Metabolism
- Fluorine in Organic Chemistry
- ATP Synthase and ATPases Research
Institute of Microbial Technology
2010-2017
Council of Scientific and Industrial Research
2011-2017
Karolinska Institutet
2016-2017
North Middlesex Hospital
2010
Middlesex University
2010
By classical competitive antagonism, a substrate and inhibitor must bind mutually exclusively to the active site. The inhibition of O-acetyl serine sulfhydrylase (OASS) by C-terminus acetyltransferase (SAT) presents paradox, because SAT binds site OASS with an affinity that is 4–6 log-fold (104–106) greater than substrate. Therefore, we employed multiple approaches understand how gains access under physiological conditions. Single-molecule ensemble showed site-bound high-affinity actively...
Fatty acids play critical role in the survival and virulence of Mycobacterium tuberculosis (Mtb). Activation fatty by acyl-CoA synthetases (Fad) into is first one crucial steps acid metabolism. Mtb possesses 36 synthetases, unlike Escherichia coli, which has single enzyme. However, mechanisms expression these multiple Fad genes regulated remain uncharacterized. We characterized DNA- ligand-binding properties a putative tetracycline repressor family regulator, named Fad35R, located upstream...
Abstract Background Methionine aminopeptidase (MetAP) is a ubiquitous enzyme in both prokaryotes and eukaryotes, which catalyzes co-translational removal of N-terminal methionine from elongating polypeptide chains during protein synthesis. It specifically removes the terminal all organisms, if penultimate residue non-bulky uncharged. The MetAP action for exclusion mandatory 50-70% nascent proteins. Such an activity required proper sub cellular localization, additional processing eventually...
In the human malaria parasite Plasmodium falciparum, membrane glutathione S-transferases (GST) have recently emerged as potential cellular detoxifying units and drug target candidates with artemisinin (ART) class of antimalarials inhibiting their activity at single-digit nanomolar potency when activated by iron sources such cytotoxic hematin. Here we put forward hypothesis that GST falciparum exported protein 1 (PfEXP1, PF3D7_1121600) might be directly involved in mode action unrelated...
Dug1p, a M20 family metallopeptidase and human orthologue of carnosinase, hydrolyzes Cys-Gly dipeptide, the last step glutathione (GSH) degradation in Saccharomyces cerevisiae. Molecular bases peptide recognition by Dug1p other peptidases remain unclear absence structural information about enzyme–peptide complexes. We report crystal structure at 2.55 Å resolution complex with Gly-Cys dipeptide two Zn2+ ions. The is trapped tunnel-like active site; its C-terminus held residues S1′ binding...