Chloroeremomycin
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Chloroeremomycin
Chloroeremomycin is a member of the glycopeptide family of antibiotics, such as vancomycin. The molecule is a non-ribosomal polypeptide that has been glycosylated. It is composed of seven amino acids and three saccharide units. Although chloroeremomycin has never been used in human medicine, oritavancin, a semi-synthetic derivative of chloroeremomycin, has full FDA approval. Chloroeremomycin is a type of glycopeptide antibiotic and works by blocking the construction of a cell wall. Chloroeremomycin is naturally produced by ''Amycolatopsis orientalis''. History Chloroeremomycin was discovered by Eli Lilly in the 1980s. In the 1990s, researchers at Eli Lilly developed biphenyl-chloroeremomycin, now known as oritavancin, as a functionalized derivative of chloroeremomycin to combat rising antibacterial resistance to vancomycin. The chloroeremomycin gene cluster was sequenced by van Wageningen ''et al'' in 1998.van Wageningen, A. M. A., Kirkpatrick, P. N., Williams, D. H., Harris, ...
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4-Hydroxyphenylglycine
4-Hydroxyphenylglycine (HPG) is a Non-proteinogenic amino acids, non-proteogenic amino acid found in vancomycin and related glycopeptides. HPG is synthesized from the Shikimate pathway, shikimic acid pathway and requires four enzymes to synthesize: Both L- and D-HPG are used in the vancomycin class of antibiotics. Tyrosine, a similar amino acid, differs by a methylene group (CH2) between the aromatic ring and the alpha carbon. Biosynthesis : HPG is synthesized from Prephenic acid, prephenate, an intermediate in the shikimic acid pathway and also a precursor to tyrosine. Prephenate is aromatized by prephenate dehydrogenase (Pdh) using Nicotinamide adenine dinucleotide, NAD+ as a cofactor to produce 4-hydroxyphenylpyruvate. 4-Hydroxyphenylpyruvate is then oxidized by 4-hydroxymandelate synthase (4HmaS) using oxygen to form 4-hydroxymandelate and hydrogen peroxide. 4HmaS is a non-heme iron-dependent dioxygenase. The reaction mechanism of this unique oxidation was proposed by Chorob ...
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