ISSN:
1432-072X
Keywords:
Methanobacterium
;
Serine transhydroxymethylase
;
Methanogen
;
Tetrahydromethanopterin
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00446773
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