2007
DOI: 10.1002/anie.200703810
|View full text |Cite
|
Sign up to set email alerts
|

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

Abstract: Third time's the charm! The structure of the phosphonate antibiotic A53868, first isolated in 1983 from Streptomyces luridus, has proven quite elusive. Originally reported as 1 and later revised to 2, the actual structure of the compound is the unusual dehydro aminophosphonic acid 3.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
23
0

Year Published

2008
2008
2024
2024

Publication Types

Select...
6
1
1

Relationship

0
8

Authors

Journals

citations
Cited by 38 publications
(23 citation statements)
references
References 42 publications
0
23
0
Order By: Relevance
“…Compound 7, a proposed structure for the antibiotic A53868, has been synthesized via a sequence of reactions involving nickel-catalyzed hydrophosphorylation of a propargyl amine derivative in the presence of diphenylphosphinic acid (Scheme 16) [21]. Although the compound is not identified with the natural A53868, it also displays antimicrobial activity against Escherichia coli.…”
Section: Hp(o)phmentioning
confidence: 99%
“…Compound 7, a proposed structure for the antibiotic A53868, has been synthesized via a sequence of reactions involving nickel-catalyzed hydrophosphorylation of a propargyl amine derivative in the presence of diphenylphosphinic acid (Scheme 16) [21]. Although the compound is not identified with the natural A53868, it also displays antimicrobial activity against Escherichia coli.…”
Section: Hp(o)phmentioning
confidence: 99%
“…Dehydrophos produced by Streptomyces luridus is unusual in that it is the only natural product phosphonate known to date in which the phosphonate group is esterified [33] (Figure 4A). Its biosynthetic gene cluster was recently sequenced revealing a candidate gene for the methyltransferase that installs the methyl ester [11].…”
Section: Biosynthesis Of Dehydrophosmentioning
confidence: 99%
“…The peptide dehydrophos is a broad‐spectrum antibiotic . This naturally occurring phosphonopeptide possesses a dehydrophosphoalanine residue at the C ‐terminal position, which is responsible for its biological activity. Thus, dehydrophos acts as a trojan horse and is taken by the target microorganism, where it is hydrolyzed to a toxic phosphopyruvate derivative after cleavage of peptide bonds .…”
Section: Introductionmentioning
confidence: 99%