PMID:1731915
| Citation |
Warren, MJ, Roessner, CA, Ozaki, S, Stolowich, NJ, Santander, PJ and Scott, AI (1992) Enzymatic synthesis and structure of precorrin-3, a trimethyldipyrrocorphin intermediate in vitamin B12 biosynthesis. Biochemistry 31:603-9 |
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| Abstract |
The trimethylated intermediate of vitamin B12 (corrin) biosynthesis, precorrin-3, was produced from various 13C-enriched isotopomers of 5-aminolevulinic acid (ALA), using a multiple-enzyme system containing ALA dehydratase, porphobilinogen deaminase, uro'gen III synthetase, and the S-adenosyl-L-methionine-(SAM)-dependent uro'gen III methyltransferase (M-1) and precorrin-2 methyltransferase (M-2) in the presence of [13C]SAM. Structural analysis of the resulting product, precorrin-3, reveals a close similarity to precorrin-2 but with several subtle differences in the conjugated array of C = C and C = N bonds which reflect the presence of the new C-methyl group at C20 and its influence on the electronic distribution in the dipyrrocorphin chromophore. The implications of this structure for corrin biosynthesis are discussed. |
| Links | |
| Keywords |
Escherichia coli/genetics; Genetic Vectors; Hydroxymethylbilane Synthase/chemistry; Magnetic Resonance Spectroscopy; Methyltransferases/chemistry; Porphobilinogen/chemistry; Porphobilinogen Synthase/chemistry; Pseudomonas/genetics; Uroporphyrinogen III Synthetase/chemistry; Uroporphyrins/biosynthesis; Uroporphyrins/chemistry; Vitamin B 12/biosynthesis; Vitamin B 12/genetics |
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