2007
DOI: 10.1038/nchembio.2007.9
|View full text |Cite
|
Sign up to set email alerts
|

Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide

Abstract: Phosphinothricin-tripeptide (PTT, phosphinothricyl-alanyl-alanine) is a natural product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus ATCC 21705 1 and Streptomyces viridochromogenes DSM 40736 2 . PTT has attracted widespread interest due to its commercial applications and unique phosphinic acid functional group. Despite intensive study since its discovery in 1972 (see 3 for a comprehensive review), a number of steps early in the PTT biosynthetic pathway remain uncharacterized. … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

3
155
0

Year Published

2007
2007
2022
2022

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 121 publications
(158 citation statements)
references
References 29 publications
3
155
0
Order By: Relevance
“…SPB78 using an rpsL dominance based counterselection strategy (28). Design and construction of deletion cassettes used to carry out the unmarked deletion of the frontalamide biosynthetic genes ftdA and ftdB were carried out as previously described (29). Detailed methods used to construct these mutants can be found in the SI Appendix.…”
Section: Methodsmentioning
confidence: 99%
“…SPB78 using an rpsL dominance based counterselection strategy (28). Design and construction of deletion cassettes used to carry out the unmarked deletion of the frontalamide biosynthetic genes ftdA and ftdB were carried out as previously described (29). Detailed methods used to construct these mutants can be found in the SI Appendix.…”
Section: Methodsmentioning
confidence: 99%
“…The pepM gene cluster of S. monomycini NRRL B-24309 suggests (Fig. 2B) that the AmPn core is synthesized from PEP by homologs of PhpA-PhpE from phosphinothricin biosynthesis (32). Putative ATP-grasp ligase and GCN5-related N-acetyltransferases (GNAT; FemXAB nonribosomal peptidyltransferase) encoded by neighboring genes may catalyze peptide bond formation.…”
Section: Dereplication Of Phosphonate Biosynthetic Pathways and Produmentioning
confidence: 99%
“…2A). Although AmPn is not a known natural product, it has been reported as an off-pathway metabolite in mutants blocked for phosphinothricin production and as a product of glyphosate degradation (32,33). N5-OH-Arg has previously been isolated as a free amino acid from strains of Bacillus cereus (34,35) and the fungus Nanniizia gypsea (Arthroderma gypseum) (36).…”
Section: Dereplication Of Phosphonate Biosynthetic Pathways and Produmentioning
confidence: 99%
“…Conjugation of nucleotides to pathway intermediates is also found in the biosynthesis of FR-900098 and phosphinothricin. In both cases, a nucleotidyltransferase transfers a CMP moiety from CTP to one of the phosphonate oxygen atoms of a biosynthetic intermediate about halfway into the overall pathway (4,27). We heterologously expressed Psf7 in E. coli and purified the protein but to date have not been able to detect any activity using a series of nucleotides and potential phosphonate substrates (fosfomycin, PnPy, Pmm, 2-oxopropionylphosphonate).…”
Section: Resultsmentioning
confidence: 99%