Investigation of serine hydroxymethyltransferase in methanogens.
The cofactor specificity of serine hydroxymethyltransferase (SHMT) activities was tested in extracts of several methanogens using tetrahydromethanopterin (H4MPt) from Methanobacterium thermoautotrophicum Marburg, tetrahydrosarcinapterin (H4SPt) from Methanosarcina barkeri, and tetrahydrofolate (H4folate) as the potential C1 carrier. In Methanosphaera stadtmanae and Methanococcus thermolithotrophicus, the activities were H4MPt dependent. In Methanospirillum hungatei GP1, Methanosaeta concilii, Methanolobus tindarius, and Methanosarcina barkeri Fusaro, the activities were strictly H4folate dependent. H4SPt was reactive with the SHMT of Methanosphaera stadtmanae but not with that of Methanosarcina barkeri. In both Methanosarcina barkeri and Methanospirillum hungatei, pyridoxal phosphate stimulated SHMT activity. The apparent K(m) values for H4folate and L-serine were 0.086 and 0.29 mM in Methanosarcina barkeri and 0.065 and 0.31 mM in Methanospirillum hungatei, respectively.
Lin
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Department of Microbiology, University of Manitoba, Winnipeg, Canada.
Sparling
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D019843:Archaeal Proteins / Q000302:isolation & purification / Q000378:metabolism; D019605:Euryarchaeota / Q000201:enzymology* / Q000254:growth & development; D005492:Folic Acid / Q000032:analysis; D012696:Glycine Hydroxymethyltransferase / Q000302:isolation & purification / Q000378:metabolism*; D011622:Pterins / Q000378:metabolism
D019843:Archaeal Proteins; D011622:Pterins; D005492:Folic Acid; D012696:Glycine Hydroxymethyltransferase