Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO2 fixation cycle in extremely thermoacidophilic archaea |
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| Affiliation: | 1. Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States;2. Dept. of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States;1. Department of Biochemistry & Molecular Biology, University of Georgia, Athens, GA 30602, USA;2. Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695, USA;1. Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China;2. Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, United States;3. School of Life Sciences, Tsinghua University, Beijing 100084, China;1. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA;2. Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA;1. Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan;2. Research Center, Asahi Glass Co., Ltd., 1150 Hazawacho, Yokohama 221-8755, Japan |
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| Abstract: | The 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle fixes CO2 in extremely thermoacidophilic archaea and holds promise for metabolic engineering because of its thermostability and potentially rapid pathway kinetics. A reaction kinetics model was developed to examine the biological and biotechnological attributes of the 3HP/4HB cycle as it operates in Metallosphaera sedula, based on previous information as well as on kinetic parameters determined here for recombinant versions of five of the cycle enzymes (malonyl-CoA/succinyl-CoA reductase, 3-hydroxypropionyl-CoA synthetase, 3-hydroxypropionyl-CoA dehydratase, acryloyl-CoA reductase, and succinic semialdehyde reductase). The model correctly predicted previously observed features of the cycle: the 35–65% split of carbon flux through the acetyl-CoA and succinate branches, the high abundance and relative ratio of acetyl-CoA/propionyl-CoA carboxylase (ACC) and MCR, and the significance of ACC and hydroxybutyryl-CoA synthetase (HBCS) as regulated control points for the cycle. The model was then used to assess metabolic engineering strategies for incorporating CO2 into chemical intermediates and products of biotechnological importance: acetyl-CoA, succinate, and 3-hydroxypropionate. |
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| Keywords: | 3-hydroxypropionate 4-hydroxybutyrate Metallosphaera sedula |
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