ENZYMATIC-SYNTHESIS AND STRUCTURE OF PRECORRIN-3, A TRIMETHYLDIPYRROCORPHIN INTERMEDIATE IN VITAMIN-B12 BIOSYNTHESIS

被引:48
作者
WARREN, MJ [1 ]
ROESSNER, CA [1 ]
OZAKI, SI [1 ]
STOLOWICH, NJ [1 ]
SANTANDER, PJ [1 ]
SCOTT, AI [1 ]
机构
[1] TEXAS A&M UNIV SYST,DEPT CHEM,CTR BIOL NMR,COLLEGE STN,TX 77843
关键词
D O I
10.1021/bi00117a043
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The trimethylated intermediate of vitamin B-12 (corrin) biosynthesis, precorrin-3, was produced from various C-13-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 [C-13]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.
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页码:603 / 609
页数:7
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