PURIFICATION AND CHARACTERIZATION OF THE ACYL CARRIER PROTEIN OF THE STREPTOMYCES-GLAUCESCENS TETRACENOMYCIN-C POLYKETIDE SYNTHASE

被引：90

作者：

SHEN, B

SUMMERS, RG

GRAMAJO, H

BIBB, MJ

HUTCHINSON, CR

机构：

[1] UNIV WISCONSIN,SCH PHARM,MADISON,WI 53706

[2] UNIV WISCONSIN,DEPT BACTERIOL,MADISON,WI 53706

[3] AFRC,INST PLANT SCI,NORWICH NR4 7UA,NORFOLK,ENGLAND

[4] JOHN INNES INST,NORWICH NR4 7UH,NORFOLK,ENGLAND

来源：

JOURNAL OF BACTERIOLOGY | 1992年 / 174卷 / 11期

关键词：

D O I：

10.1128/JB.174.11.3818-3821.1992

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The acyl carrier protein (ACP) of the tetracenomycin C polyketide synthase, encoded by the tcmM gene, has been expressed in both Streptomyces glaucescens and Escherichia coli and purified to homogeneity. Expression of the tcmM gene in E. coli results mainly in the TcmM apo-ACP, whereas expression in S. glaucescens yields solely the holo-ACP. The purified holo-TcmM is active in a malonyl coenzyme A:ACP transacylase assay and is labeled by radioactive beta-alanine, confirming that it carries a 4'-phosphopantetheine prosthetic group.

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页码：3818 / 3821

页数：4

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