Abstract
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.
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Hoyt, J.C., Oren, A., Escalante-Semerena, J.C. et al. Tetrahydromethanopterin-dependent serine transhydroxymethylase from Methanobacterium thermoautotrophicum . Arch. Microbiol. 145, 153–158 (1986). https://doi.org/10.1007/BF00446773
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DOI: https://doi.org/10.1007/BF00446773