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N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri

MPS-Authors

Klein,  A. R.
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Breitung,  J.
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  R. K.       
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Klein, A. R., Breitung, J., Linder, D., Stetter, K. O., & Thauer, R. K. (1993). N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri. Archives of Microbiology, 159(3), 213-219. doi:10.1007/BF00248474.


Cite as: https://hdl.handle.net/21.11116/0000-000F-9146-E
Abstract
Archaeoglobus fulgidus and Methanopyrus kandleri are both extremely thermophilic Archaea with a growth temperature optimum at 83°C and 98°C, respectively. Both Archaea contain an active N5,N10-methenyltetrahydromethanopterin cyclohydrolase. The enzyme from M. kandleri has recently been characterized. We describe here the purification and properties of the enzyme from A. fulgidus.