PURIFICATION AND CHARACTERIZATION OF A NOVEL ENOYL COENZYME-A REDUCTASE FROM STREPTOMYCES-COLLINUS

被引：23

作者：

REYNOLDS, KA ^{[1
]}

WANG, P ^{[1
]}

FOX, KM ^{[1
]}

SPEEDIE, MK ^{[1
]}

LAM, Y ^{[1
]}

FLOSS, HG ^{[1
]}

机构：

[1] UNIV WASHINGTON,DEPT CHEM,SEATTLE,WA 98195

来源：

JOURNAL OF BACTERIOLOGY | 1992年 / 174卷 / 12期

关键词：

D O I：

10.1128/jb.174.12.3850-3854.1992

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A novel NADPH-dependent enoyl reductase, catalyzing the conversion of 1-cyclohexenylcarbonyl coenzyme A (1-cyclohexenylcarbonyl-CoA) to cyclohexenylcarbonyl-CoA, was purified to homogeneity from Streptomyces collinus. This enzyme, a dimer with subunits of identical M(r) (36,000), exhibits a K(m) of 1.5 +/- 0.3-mu-M for NADPH and 25 +/- 3-mu-M for 1-cyclohexenylcarbonyl-CoA. It has a pH optimum of 7.5, is most active at 30-degrees-C, and is inhibited by both divalent cations and thiol reagents. Two internal peptide sequences were obtained. Ansatrienin A (an antibiotic produced by S. collinus) contains a cyclohexanecarboxylic acid moiety, and it is suggested that the 1-cyclohexenylcarbonyl-CoA reductase described herein catalyzes the final reductive step in the conversion of shikimic acid into this moiety.

引用

页码：3850 / 3854

页数：5

共 33 条

[1] STEREOCHEMISTRY OF THE REACTIONS CATALYZED BY CHICKEN LIVER FATTY-ACID SYNTHASE [J].