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  Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri

Shima, S., & Thauer, R. K. (2001). Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri. HYPERTHERMOPHILIC ENZYMES, PT B, 317-353. doi:10.1016/S0076-6879(01)31069-8.

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 Creators:
Shima, Seigo1, Author           
Thauer, Rudolf K.2, Author           
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1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              
2Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311              

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 Abstract: Methanopyrus kandleri is a hyperthermophilic archaeon growing optimally at 98° on H2 and CO2 with the formation of CH4. The organism belonging to the kingdom of Euryarchaeota is the most thermophilic methanogen known so far and is phylogenetically only distantly related to all other known methanogens. The pathway of CO2 reduction to CH4 in M. kandleri has been shown to be identical to that used in all other methanogens. It involves six tetrahydromethanopterin-specific enzymes. Tetrahydromethanopterin (H4MPT) is a tetrahydrofolate analog. This chapter describes the purification, assay, and properties of the five characterized H4MPT-specific enzymes from M. kandleri. It also provides a description of the isolation of the coenzymes required to assay these enzymes.

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 Dates: 2001
 Publication Status: Issued
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Title: HYPERTHERMOPHILIC ENZYMES, PT B
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 317 - 353 Identifier: ISSN: 0076-6879

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Title: Methods inEnzymology
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Publ. Info: Elsevier
Pages: - Volume / Issue: 331 Sequence Number: - Start / End Page: - Identifier: -