Overproduction of α-Lipoic Acid by Gene Manipulated Escherichia coli

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منابع مشابه

Overproduction of α-Lipoic Acid by Gene Manipulated Escherichia coli

Alpha-lipoic acid (LA) is an important enzyme cofactor widely used by organisms and is also a natural antioxidant for the treatment of pathologies driven by low levels of endogenous antioxidants. In order to establish a safer and more efficient process for LA production, we developed a new biological method for LA synthesis based on the emerging knowledge of lipoic acid biosynthesis. We first c...

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Expression of the porcine lipoic acid synthase (LIAS) gene in Escherichia coli.

Lipoic acid synthase, which exists primarily in mitochondria, participates in the biosynthesis of intrinsic lipoic acid. The lipoic acid synthase gene in pig is known as LIAS. To further investigate the biological functions of the protein that is encoded by LIAS, we cloned the open read frame of porcine LIAS (GenBank No. JN797612.1) into the expression vector pET-28α(+). The resulting pET-28α(+...

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Amelioration of docetaxel/cisplatin induced polyneuropathy by α-lipoic acid

Docetaxel (Taxotere; Aventis, Strasbourg, France) is currently considered to be one of the most important anticancer drugs. It is a semi-synthetic agent derived from baccatin III extracted from renewable Taxus baccata needles, which binds to tubulin inducing its polymerization [1]. It inhibits cell replication and leads to apoptosis. Docetaxel has displayed significant antitumor activity agains...

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Overproduction of Clavulanic Acid by UV Mutagenesis of Streptomyces clavuligerus

Clavulanic acid is produced industrially by fermentation of Streptomyces clavuligerus and researches have increased its production by strain improvement, recombinant DNA technology, and media composition and growth condition optimization. The main objective of this study was to increase the level of clavulanic acid production from Streptomyces clavuligerus (DSM 738), using UV irradiation. After...

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Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.

Amino-acid sequences around two lipoic acid residues in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli were investigated. A single amino acid sequence of 13 residues was found. A repeated amino acid sequence in the lipoate acetyltransferase chain might explain this result.

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ژورنال

عنوان ژورنال: PLOS ONE

سال: 2017

ISSN: 1932-6203

DOI: 10.1371/journal.pone.0169369