lankacidins and glyceric-acid

lankacidins has been researched along with glyceric-acid* in 1 studies

Other Studies

1 other study(ies) available for lankacidins and glyceric-acid

Article	Year
An unusual dehydratase acting on glycerate and a ketoreducatse stereoselectively reducing α-ketone in polyketide starter unit biosynthesis. Angewandte Chemie (International ed. in English), 2014, Oct-13, Volume: 53, Issue:42 Polyketide synthases (PKSs) usually employ a ketoreductase (KR) to catalyze the reduction of a β-keto group, followed by a dehydratase (DH) that drives the dehydration to form a double bond between the α- and β-carbon atoms. Herein, a DH-KR involved in FR901464 biosynthesis was characterized: DH* acts on glyceryl-S-acyl carrier protein (ACP) to yield ACP-linked pyruvate; subsequently KR* reduces α-ketone that yields L-lactyl-S-ACP as starter unit for polyketide biosynthesis. Genetic and biochemical evidence was found to support a similar pathway that is involved in the biosynthesis of lankacidins. These results not only identified new PKS domains acting on different substrates, but also provided additional options for engineering the PKS starter pathway or biocatalysis. Topics: Acyl Carrier Protein; Antineoplastic Agents; Bacterial Proteins; Biosynthetic Pathways; Escherichia coli; Glyceric Acids; Hydro-Lyases; Ketones; Macrolides; Polyketide Synthases; Pyrans; Spiro Compounds; Streptomyces; Substrate Specificity	2014

Article

Year

An unusual dehydratase acting on glycerate and a ketoreducatse stereoselectively reducing α-ketone in polyketide starter unit biosynthesis.

Angewandte Chemie (International ed. in English), 2014, Oct-13, Volume: 53, Issue:42

Polyketide synthases (PKSs) usually employ a ketoreductase (KR) to catalyze the reduction of a β-keto group, followed by a dehydratase (DH) that drives the dehydration to form a double bond between the α- and β-carbon atoms. Herein, a DH*-KR* involved in FR901464 biosynthesis was characterized: DH* acts on glyceryl-S-acyl carrier protein (ACP) to yield ACP-linked pyruvate; subsequently KR* reduces α-ketone that yields L-lactyl-S-ACP as starter unit for polyketide biosynthesis. Genetic and biochemical evidence was found to support a similar pathway that is involved in the biosynthesis of lankacidins. These results not only identified new PKS domains acting on different substrates, but also provided additional options for engineering the PKS starter pathway or biocatalysis.

Topics: Acyl Carrier Protein; Antineoplastic Agents; Bacterial Proteins; Biosynthetic Pathways; Escherichia coli; Glyceric Acids; Hydro-Lyases; Ketones; Macrolides; Polyketide Synthases; Pyrans; Spiro Compounds; Streptomyces; Substrate Specificity

2014