Allokairic Regulation Of Enzyme Function | 63551
ISSN: 2155-952X

Journal of Biotechnology & Biomaterials
Open Access

Like us on:

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
Recommended Conferences

2nd International Conference on Biotechnology and Healthcare

Auckland, New Zealand
Google scholar citation report
Citations : 1536

Journal of Biotechnology & Biomaterials received 1536 citations as per google scholar report

Indexed In
  • Index Copernicus
  • Google Scholar
  • Sherpa Romeo
  • Open J Gate
  • Genamics JournalSeek
  • Academic Keys
  • ResearchBible
  • China National Knowledge Infrastructure (CNKI)
  • Access to Global Online Research in Agriculture (AGORA)
  • Electronic Journals Library
  • RefSeek
  • Hamdard University
  • OCLC- WorldCat
  • SWB online catalog
  • Virtual Library of Biology (vifabio)
  • Publons
  • Geneva Foundation for Medical Education and Research
  • Euro Pub
Share This Page

Allokairic regulation of enzyme function

Joint Event on 15th World Congress on Biotechnology And Biotech Industries Meet and 2nd International Conference on Enzymology and Molecular Biology

Brian G Miller

Florida State University, USA

ScientificTracks Abstracts: J Biotechnol Biomater

DOI: 10.4172/2155-952X.C1.070

Human glucokinase (GCK), the body’s primary glucose sensor and a major determinant of glucose homeostatic diseases, displays a unique form of allosteric-like behavior that is manifested as a cooperative kinetic response to glucose. The allosteric-like behavior of GCK is particularly intriguing since the enzyme is monomeric and contains only one glucose binding site. Recent work in our laboratory has shown that millisecond timescale order-disorder transitions within the enzyme’s small domain govern cooperativity. Here, we present the results of biophysical studies that elucidate the structural and dynamic origins of the timedependent, allokairic properties of GCK. Using high-resolution nuclear magnetic resonance, we identify two distinct mechanisms by which GCK can be activated, both of which result in hyperinsulinemia. The first activation mechanism alters the equilibrium distribution of GCK conformers in favor of a single-state, whereas the second mechanism alters the intrinsic dynamics of the enzyme without perturbing the relative distribution of states in the structural ensemble. Time-resolved fluorescence measurements map the dynamic conformational landscape of GCK and provide evidence for three distinct conformations of the enzyme in the absence of glucose. Together our findings provide a framework for understanding the origins of time-dependent changes in activity in other regulatory enzymes.

Brian Miller is an Associate Professor of Biochemistry at the Florida State University, USA. He did his PhD from the University of North Carolina, Chapel Hill in the year 2001. His research interest is protein structure, function and evolution.

Email: [email protected]