MULTIENZYME SYNTHESIS AND STRUCTURE OF FACTOR-S3

被引：15

作者：

OZAKI, SI

ROESSNER, CA

STOLOWICH, NJ

ATSHAVES, BP

HERTLE, R

MULLER, G

SCOTT, AI

机构：

[1] TEXAS A&M UNIV SYST,CTR BIOL NMR,DEPT CHEM,COLL STN,TX 77843

[2] UNIV STUTTGART,INST ORGAN CHEM BIOCHEM & ISOTOPENFORSCH,W-7000 STUTTGART 1,GERMANY

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 1993年 / 115卷 / 18期

关键词：

D O I：

10.1021/ja00071a001

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Factor S3, an unusual metabolite of Propionibacterium shermanii, is biosynthesized from porphobilinogen (PBG) by three enzymes, PBG deaminase, uro'gen III methyltransferase (M1), and the Salmonella typhimurium cbiF gene product, isolated from recombinant strains of Escherichia coli. PBG deaminase affords uro'gen I, and M1 performs the methylation of three beta-pyrrolic carbons of uro'gen I to form 2,7,12-trimethylpyrrocorphin I. The cbiF gene product then methylates one alpha-pyrrolic carbon (C-16). Nonenzymatic insertion of zinc into the macrocycle forms the tetramethylated zinc corphinoid factor S3.

引用

页码：7935 / 7938

页数：4

共 17 条

[1] ASSAY, PURIFICATION, AND CHARACTERIZATION OF COBALTOCHELATASE, A UNIQUE COMPLEX ENZYME CATALYZING COBALT INSERTION IN HYDROGENOBYRINIC ACID A,C-DIAMIDE DURING COENZYME B-12 BIOSYNTHESIS IN PSEUDOMONAS-DENITRIFICANS [J].