Tetrahydromethanopterin-dependent serine transhydroxymethylase from Methanobacterium thermoautotrophicum

J. C. Hoyt, A. Oren, J. C. Escalante-Semerena, R. S. Wolfe*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Serine transhydroxymethylase of Methanobacterium thermoautotrophicum has been purified to within 95% of homogeneity. Activity was strictly dependent on tetrahydromethanopterin, tetrahydrofolate being unable to serve as the acceptor C1 units from l-serine. The native protein has a molecular weight of about 102,000 daltons. The enzyme shows maximal activity at 60°C, has a pH optimum of 8.1, and required pyridoxal-5′-phosphate and Mg2+ for optimal activity.

Original languageAmerican English
Pages (from-to)153-158
Number of pages6
JournalArchives of Microbiology
Issue number2
StatePublished - Jul 1986
Externally publishedYes


  • Methanobacterium
  • Methanogen
  • Serine transhydroxymethylase
  • Tetrahydromethanopterin


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