6-deoxyerythronolide B

6-deoxyerythronolide B is a lipid of Polyketides (PK) class. The involved functions are known as Anabolism, Biosynthetic Pathways and Synthesis. The associated genes with 6-deoxyerythronolide B are LARGE gene. The related lipids are Propionate.

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Introduction

To understand associated biological information of 6-deoxyerythronolide B, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with 6-deoxyerythronolide B?

There are no associated biomedical information in the current reference collection.

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with 6-deoxyerythronolide B

Lipid pathways are not clear in current pathway databases. We organized associated pathways with 6-deoxyerythronolide B through full-text articles, including metabolic pathways or pathways of biological mechanisms.

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PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with 6-deoxyerythronolide B?

There are no associated biomedical information in the current reference collection.

What functions are associated with 6-deoxyerythronolide B?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with 6-deoxyerythronolide B?

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What genes are associated with 6-deoxyerythronolide B?

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Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with 6-deoxyerythronolide B?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with 6-deoxyerythronolide B

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Authors Title Published Journal PubMed Link
Leaf T et al. Precursor-directed biosynthesis of 6-deoxyerythronolide B analogs in Streptomyces coelicolor: understanding precursor effects. 2000 Jul-Aug Biotechnol. Prog. pmid:10933827
Desai RP et al. Combining classical, genetic, and process strategies for improved precursor-directed production of 6-deoxyerythronolide B analogues. 2004 Jan-Feb Biotechnol. Prog. pmid:14763821
Pistorino M and Pfeifer BA Efficient experimental design and micro-scale medium enhancement of 6-deoxyerythronolide B production through Escherichia coli. 2009 Sep-Oct Biotechnol. Prog. pmid:19634176
Lombó F et al. Enhancing the atom economy of polyketide biosynthetic processes through metabolic engineering. 2001 Jul-Aug Biotechnol. Prog. pmid:11485419
Zhang H et al. Investigating the role of native propionyl-CoA and methylmalonyl-CoA metabolism on heterologous polyketide production in Escherichia coli. 2010 Biotechnol. Bioeng. pmid:19806677
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Boghigian BA et al. Multi-factorial engineering of heterologous polyketide production in Escherichia coli reveals complex pathway interactions. 2011 Biotechnol. Bioeng. pmid:21337322
Meng HL et al. Construction of polyketide overproducing Escherichia coli strains via synthetic antisense RNAs based on in silico fluxome analysis and comparative transcriptome analysis. 2016 Biotechnol J pmid:26709503
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Kim C et al. The role of serine-246 in cytochrome P450eryF-catalyzed hydroxylation of 6-deoxyerythronolide B. 2001 Biosci. Biotechnol. Biochem. pmid:11388449
Yin Y et al. Erythromycin biosynthesis. The 4-pro-S hydride of NADPH is utilized for ketoreduction by both module 5 and module 6 of the 6-deoxyerythronolide B synthase. 2001 Bioorg. Med. Chem. Lett. pmid:11412964
Sharma KK and Boddy CN The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates. 2007 Bioorg. Med. Chem. Lett. pmid:17428661
Jacobsen JR et al. Precursor-directed biosynthesis of 12-ethyl erythromycin. 1998 Bioorg. Med. Chem. pmid:9784859
Argyropoulos P et al. Towards a characterization of the structural determinants of specificity in the macrocyclizing thioesterase for deoxyerythronolide B biosynthesis. 2016 Biochim. Biophys. Acta pmid:26592346
Jacobsen JR et al. Spontaneous priming of a downstream module in 6-deoxyerythronolide B synthase leads to polyketide biosynthesis. 1998 Biochemistry pmid:9538011
Lau J et al. Dissecting the role of acyltransferase domains of modular polyketide synthases in the choice and stereochemical fate of extender units. 1999 Biochemistry pmid:9931032
Tsuji SY et al. Selective protein-protein interactions direct channeling of intermediates between polyketide synthase modules. 2001 Biochemistry pmid:11327852
Tsai SC et al. Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases. 2002 Biochemistry pmid:12379102
Murli S et al. Identification of domains within megalomicin and erythromycin polyketide synthase modules responsible for differences in polyketide production levels in Escherichia coli. 2004 Biochemistry pmid:15595843
Yuzawa S et al. Role of a conserved arginine residue in linkers between the ketosynthase and acyltransferase domains of multimodular polyketide synthases. 2012 Biochemistry pmid:22509729