Article The Peculiar Glycolytic Pathway in Hyperthermophylic Archaea: Understanding Its Whims by Experimentation In Silico Yanfei Zhang 1, Theresa Kouril 2,3, Jacky L. Snoep 3,4,5, Bettina Siebers 2, Matteo Barberis 1 and Hans V. Westerhoff 1,4,5,* 1 Synthetic Systems Biology and Nuclear Organization, Swammerdam Institute for Life Sciences, University of Amsterdam, 1098 XH Amsterdam, The Netherlands;
[email protected] (Y.Z.);
[email protected] (M.B.) 2 Molecular Enzyme Technology and Biochemistry (MEB), Biofilm Centre, Centre for Water and Environment Research (CWE), University Duisburg—Essen, Universitätsstr. 5, 45141 Essen, Germany;
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[email protected] (B.S.) 3 Department of Biochemistry, University of Stellenbosch, Stellenbosch 7602, South Africa;
[email protected] 4 The Manchester Centre for Integrative Systems Biology, Manchester Institute for Biotechnology, School for Chemical Engineering and Analytical Science, University of Manchester, Manchester M1 7DN, UK 5 Department of Molecular Cell Physiology, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands * Correspondence:
[email protected]; Tel.: +31-20-598-7230 Academic Editor: Samuel De Visser Received: 12 March 2017; Accepted: 13 April 2017; Published: 20 April 2017 Abstract: Mathematical models are key to systems biology where they typically describe the topology and dynamics of biological networks, listing biochemical entities and their relationships with one another. Some (hyper)thermophilic Archaea contain an enzyme, called non- phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN), which catalyzes the direct oxidation of glyceraldehyde-3-phosphate to 3-phosphoglycerate omitting adenosine 5′-triphosphate (ATP) formation by substrate-level-phosphorylation via phosphoglycerate kinase.