Recent advances in elucidation of biological corrinoid functions.
Eleven adenosylcorrinoid-dependent rearrangements and elimination reactions have been described during the last four decades of vitamin B12 research. In contrast, only the cobamide-dependent methionine synthase was well established as a corrinoid-dependent methyl transfer reaction. yet, investigations during the last few years revealed nine additional corrinoid-dependent methyltransferases. Many of these reactions are catalyzed by bacteria which possess a distinct C1 metabolism. Notably acetogenic and methanogenic bacteria carry out such methyl transfers in their anabolism and catabolism. Tetrahydrofolate or a similar pterine derivative is a key intermediate in these reactions. It functions as methyl acceptor and the methylated tetrahydrofolate serves as a methyl donor.
Stupperich
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Department of Applied Microbiology, University of Ulm, FRG.
D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / Q000378:metabolism; D000085:Acetates / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism; D045728:Corrinoids; D019605:Euryarchaeota / Q000378:metabolism; D006801:Humans; D008697:Methane / Q000378:metabolism; D008780:Methyltransferases / Q000378:metabolism*; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism*; D013763:Tetrahydrofolates / Q000378:metabolism*
D000085:Acetates; D045728:Corrinoids; D011166:Porphyrins; D013763:Tetrahydrofolates; D008780:Methyltransferases; D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; D008697:Methane; C005984:5-methyltetrahydrofolate