Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri |
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| Authors: | Seigo Shima David A Hérault Albrecht Berkessel R K Thauer |
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| Institution: | Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Strasse, D-35043 Marburg and Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universit?t, Karl-von-Frisch-Strasse, D-35032 Marburg, Germany e-mail: thauer@mailer.uni-marburg.de Tel. +49 6421-178200; Fax +49 6421-178209, DE
Institut für Organische Chemie, Universit?t K?ln, Greinstrasse 4, D-50939 K?ln, Germany, DE
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| Abstract: | Enzymes involved in methane formation from carbon dioxide and dihydrogen in Methanopyrus kandleri require high concentrations (> 1 M) of lyotropic salts such as K2HPO4/KH2PO4 or (NH4)2SO4 for activity and for thermostability. The requirement correlates with high intracellular concentrations of cyclic 2,3-diphosphoglycerate
(cDPG; ≈ 1 M) in this hyperthermophilic organism. We report here on the effects of potassium cDPG on the activity and thermostability
of the two methanogenic enzymes cyclohydrolase and formyltransferase and show that at cDPG concentrations prevailing in the
cells the investigated enzymes are highly active and completely thermostable. At molar concentrations also the potassium salts
of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cDPG, were found to confer activity and thermostability
to the enzymes. Thermodynamic arguments are discussed as to why cDPG, rather than these salts, is present in high concentrations
in the cells of Mp. kandleri.
Received: 18 June 1998 / Accepted: 24 August 1998 |
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| Keywords: | Methanogenic archaea Formyltransferase Cyclohydrolase N5 N10-Methenyltetrahydromethanopterin Formylmethanofuran Halophilic enzymes Thermophilic enzymes 2-Phosphoglycerate kinase Cyclic diphosphoglycerate synthase |
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