A5008511786- Biochemical Acid Research Studies
- Metabolism and Genetic Disorders
- Amino Acid Enzymes and Metabolism
- Alcoholism and Thiamine Deficiency
- Biochemical and Molecular Research
- Chemical and Physical Properties in Aqueous Solutions
- Diverse Aspects of Tourism Research
- Digital Marketing and Social Media
- Analytical Chemistry and Chromatography
- Quality and Supply Management
- Enzyme Structure and Function
- Electrolyte and hormonal disorders
- Pharmacological Effects of Natural Compounds
- Consumer Behavior in Brand Consumption and Identification
- Crystallization and Solubility Studies
Maharashtra State Board of Technical Education
2020
Rutgers, The State University of New Jersey
2007-2010
Rutgers Sexual and Reproductive Health and Rights
2007
Protein motions are ubiquitous and intrinsically coupled to catalysis. Their specific roles, however, remain largely elusive. Dynamic loops at the active center of E1 component Escherichia coli pyruvate dehydrogenase multienzyme complex essential for several catalytic functions starting from a predecarboxylation event culminating in transfer acetyl moiety E2 component. Monitoring kinetics its loop variants various solution viscosities, we show that rate chemical step is modulated by...
Our crystallographic studies have shown that two active center loops (an inner loop formed by residues 401-413 and outer 541-557) of the E1 component Escherichia coli pyruvate dehydrogenase complex become organized only on binding a substrate analog is capable forming stable thiamin diphosphate-bound covalent intermediate. We showed residue His-407 has key role in mechanism, especially reductive acetylation E. dihydrolipoamide transacetylase component, whereas results this disorder-order...
Most bacterial pyruvate dehydrogenase complexes from either gram-positive or gram-negative bacteria have E1 components with an alpha(2) homodimeric quaternary structure. In a sequel to our previous publications, we present the first NMR study on flexible regions of component Escherichia coli and its biological relevance. We report sequence-specific assignments for 6 residues in N-terminal 1-55 region glycine each two mobile active center loops component, 200-kDa homodimer. This was...
Cooperativity is extensively used by enzymes, particularly those acting at key metabolic branch points, to "fine tune" catalysis. Thus, cooperativity and enzyme catalysis are intimately linked, yet their linkage poorly understood. Here we show that negative in the rate-determining step E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex an outcome redistribution a "rate-promoting" conformational pre-equilibrium. An array biophysical biochemical studies indicates...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTButynediol synthesis. A kinetic studyS. S. Kale, R. V. Chaudhari, and P. A. RamachandranCite this: Ind. Eng. Chem. Prod. Res. Dev. 1981, 20, 2, 309–315Publication Date (Print):June 1, 1981Publication History Published online1 May 2002Published inissue 1 June 1981https://pubs.acs.org/doi/10.1021/i300002a015https://doi.org/10.1021/i300002a015research-articleACS PublicationsRequest reuse permissionsArticle Views469Altmetric-Citations10LEARN ABOUT...
Sequence‐specific NMR assignments were made for six residues in the N‐terminal 1–55 region, and one each of inner (401–413) outer (541–557) active center loops E1 component E. coli pyruvate dehydrogenase complex (E1ec, 2x100 kDa), flexible regions not seen x‐ray structure. The 2D HSQC spectrum revealed 103 resonances 109 expected three regions. Site‐specific substitutions appropriate labeling patterns assisted assignments. Resonances assigned to region diminished size/were absent presence...
Dynamic active site inner and outer loops (spanning 401–413 541–557) in the E. coli pyruvate dehydrogenase multienzyme complex E1 subunit undergo disorder to order transformation presence of an intermediate analogue (Arjunan et al., J.Biol.Chem. 2006). This activity is essential for catalysis by E1and intersubunit communication with E2. Crystallographic studies indicate that H407, a multifunctional amino acid residue on loop, ordering both loops. D549 loop within hydrogen bonding distance...
The crystal structure of the E1 subunit pyruvate dehydrogenase complex from E. coli (PDHc-E1) revealed three regions low electron density, spanning residues 1–55, 401–413 and 541–557 (Arjunan et al., Biochemistry 2002, 41, 5213–5221). Region 1–55 has been shown to interact with PDHc-E2 (Park al, 2004, 43, 14037–14046) while region a role in reductive acetylation lipoamide (Nemeria 15459–15467). Studies using site specific labeling (SSL) thiol-directed probes sensitive their local environment...