Enzymes
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- Name help_outline Co-precorrin-3 Identifier CHEBI:60060 Charge -8 Formula C43H40CoN4O16 InChIKeyhelp_outline FKTVLCPLZMVWHD-LPFAUARPSA-E SMILEShelp_outline CC1=C2[N+]3=C(C=C4N5C(=CC6=[N+]7C(Cc8c(CCC([O-])=O)c(CC([O-])=O)c1n8[Co--]357)=C(CCC([O-])=O)C6CC([O-])=O)[C@@H](CCC([O-])=O)[C@]4(C)CC([O-])=O)[C@@H](CCC([O-])=O)[C@]2(C)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline Co-precorrin-4 Identifier CHEBI:60061 Charge -7 Formula C44H43CoN4O16 InChIKeyhelp_outline VHHGJROBFDFFAE-QTESGACZSA-F SMILEShelp_outline CC1OC(=O)C[C@@]2(C)[C@H](CCC([O-])=O)C3=CC4=[N+]5C(=Cc6c(CC([O-])=O)c(CCC([O-])=O)c7CC8=[N+]9C(=C(CC([O-])=O)[C@@]8(C)CCC([O-])=O)C12N3[Co--]59n67)[C@@H](CCC([O-])=O)[C@]4(C)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 768 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:26273 | RHEA:26274 | RHEA:26275 | RHEA:26276 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway.
Santander P.J., Kajiwara Y., Williams H.J., Scott A.I.
Investigation on the use of the oxidized form (factor 3 (3a)) of the trimethylated intermediate (precorrin 3 (2)) as a substrate for the enzymes of the anaerobic pathway to vitamin B12 led to the synthesis of three pairs of novel cobalt corrinoids. The products were made with the aid of the Salmon ... >> More
Investigation on the use of the oxidized form (factor 3 (3a)) of the trimethylated intermediate (precorrin 3 (2)) as a substrate for the enzymes of the anaerobic pathway to vitamin B12 led to the synthesis of three pairs of novel cobalt corrinoids. The products were made with the aid of the Salmonella typhimurium enzymes CbiH, CbiF, CbiG, and CbiT, were synthesized in several 13C labeled versions, and were isolated as methylesters after esterification. Structures were determined by detailed NMR and MS analyses. Each set of products was obtained in the decarboxylated (RMe) and non-decarboxylated (R=CH2COOCH3) forms (at the C-12 position of the porphyrinoid). << Less
Bioorg. Med. Chem. 14:724-731(2006) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Biosynthesis of vitamin B12: factor IV, a new intermediate in the anaerobic pathway.
Scott A.I., Stolowich N.J., Wang J., Gawatz O., Fridrich E., Muller G.
The structure of a novel tetradehydrocorrin, factor IV, isolated from Propionibacterium shermanii has been established by multidimensional NMR spectroscopy. Incorporation of radiolabeled factor IV into cobyrinic acid established the biointermediacy of this cobalt complex, whose structure has impli ... >> More
The structure of a novel tetradehydrocorrin, factor IV, isolated from Propionibacterium shermanii has been established by multidimensional NMR spectroscopy. Incorporation of radiolabeled factor IV into cobyrinic acid established the biointermediacy of this cobalt complex, whose structure has implications for the mechanisms of the anaerobic pathway to B12. << Less
Proc Natl Acad Sci U S A 93:14316-14319(1996) [PubMed] [EuropePMC]