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Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli.

Transcarboxylase from Propionibacterium shermanii is a complex biotin-containing enzyme composed of 30 polypeptides of three different types: a hexameric central 12S subunit to which 6 outer 5S subunits are attached through 12 1.3S biotinyl subunits. The enzyme catalyzes a two-step reaction in which...

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書目詳細資料
發表在:	J Bacteriol
Principais autores:	Thornton, C G, Kumar, G K, Haase, F C, Phillips, N F, Woo, S B, Park, V M, Magner, W J, Shenoy, B C, Wood, H G, Samols, D
格式:	Artigo
語言:	Inglês
出版:	American Society for Microbiology (ASM) 1993
主題:	Research Article
在線閱讀:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC206582/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8366018/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.175.17.5301-5308.1993
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Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli.

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