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浅青紫链霉菌四环素霉素C聚酮合酶酰基载体蛋白的纯化与特性分析

Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens tetracenomycin C polyketide synthase.

作者信息

Shen B, Summers R G, Gramajo H, Bibb M J, Hutchinson C R

机构信息

School of Pharmacy, University of Wisconsin, Madison 53706.

出版信息

J Bacteriol. 1992 Jun;174(11):3818-21. doi: 10.1128/jb.174.11.3818-3821.1992.

DOI:10.1128/jb.174.11.3818-3821.1992
PMID:1592832
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC206074/
Abstract

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.

摘要

由tcmM基因编码的四环素霉素C聚酮合酶的酰基载体蛋白（ACP）已在浅青紫链霉菌和大肠杆菌中表达，并纯化至同质。tcmM基因在大肠杆菌中的表达主要产生TcmM脱辅基ACP，而在浅青紫链霉菌中的表达仅产生全酶形式的ACP。纯化后的全酶形式的TcmM在丙二酰辅酶A：ACP转酰基酶测定中具有活性，并且被放射性β-丙氨酸标记，证实它携带一个4'-磷酸泛酰巯基乙胺辅基。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/322a/206074/6844b5919326/jbacter00077-0412-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/322a/206074/6844b5919326/jbacter00077-0412-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/322a/206074/6844b5919326/jbacter00077-0412-a.jpg

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