Journal article

Publication year: 1996

Pages: 187-193

Journal: Archives of Microbiology

Volume number: 165

Issue number: 3

ISSN: 0302-8933

DOI Link: https://doi.org/10.1007/s002030050314

Publisher: Springer

Abstract: 
H-2-Forming N-5,N-10-methylenetetrahydromethanopterin dehydrogenase (Hmd) is a novel type of hydrogenase found in methanogenic Achaea that contains neither nickel nor iron-sulfur clusters. The enzyme has previously been characterized from Methanobacterium thermoautotrophicum and from Methanopyrus kandleri. We report here on the purification and properties of the enzyme from Methanococcus thermolithotrophicus. The hmd gene was cloned and sequenced. The results indicate that the enzyme from Me. thermolithotrophicus is functionally and structurally closely related to the H-2-forming methylene tetrahydromethanopterin dehydrogenase from Mh. thermoautotrophicum and Mp. kandleri. From amino acid sequence comparisons of the three enzymes, a phylogenetic tree was deduced that shows branching orders similar to those derived from sequence comparisons of the 16S rRNA of the orders Methanococcales, Methanobacteriales, and Methanopyrales.

Harvard Citation style: Hartmann, G., Klein, A., Linder, M. and Thauer, R. (1996) Purification, properties and primary structure of H-2-forming N-5,N(10)methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus, Archives of Microbiology, 165(3), pp. 187-193. https://doi.org/10.1007/s002030050314

APA Citation style: Hartmann, G., Klein, A., Linder, M., & Thauer, R. (1996). Purification, properties and primary structure of H-2-forming N-5,N(10)methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus. Archives of Microbiology. 165(3), 187-193. https://doi.org/10.1007/s002030050314