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Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli.

作者信息

Neale A D, Scopes R K, Wettenhall R E, Hoogenraad N J

出版信息

J Bacteriol. 1987 Mar;169(3):1024-8. doi: 10.1128/jb.169.3.1024-1028.1987.

DOI:10.1128/jb.169.3.1024-1028.1987
PMID:3546263
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC211896/
Abstract

Pyruvate decarboxylase (EC 4.1.1.1) from Zymomonas mobilis purified to homogeneity by using dye-ligand and ion-exchange chromatography. Antibodies produced against the enzyme and the amino-terminal sequence obtained for the pure enzyme were used to select and confirm the identity of a genomic clone encoding the enzyme selected from a genomic library of Z. mobilis DNA cloned into pUC9. The genomic fragment encoding the enzyme expressed high levels of pyruvate decarboxylase in Escherichia coli. Possible RNA polymerase and ribosome-binding sites have been identified in the 5'-untranslated region of the pyruvate decarboxylase gene.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b7b0/211896/6f155a783901/jbacter00193-0110-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b7b0/211896/6f155a783901/jbacter00193-0110-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b7b0/211896/6f155a783901/jbacter00193-0110-a.jpg

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Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli.
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PREPARATION OF TRANSFORMING DEOXYRIBONUCLEIC ACID BY PHENOL TREATMENT.通过苯酚处理制备转化脱氧核糖核酸
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