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PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis.
- Source :
-
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2019 Nov 28; Vol. 55 (96), pp. 14502-14505. - Publication Year :
- 2019
-
Abstract
- ForI is a PLP-dependent enzyme from the biosynthetic pathway of the C-nucleoside antibiotic formycin. Cycloserine is thought to inhibit PLP-dependent enzymes by irreversibly forming a PMP-isoxazole. We now report that ForI forms novel PMP-diketopiperazine derivatives following incubation with both d and l cycloserine. This unexpected result suggests chemical diversity in the chemistry of cycloserine inhibition.
- Subjects :
- Bacterial Proteins antagonists & inhibitors
Bacterial Proteins genetics
Biocatalysis
Catalytic Domain
Cycloserine chemistry
Diketopiperazines metabolism
Formycins chemistry
Hydrogen-Ion Concentration
Pyridoxamine chemistry
Pyridoxamine metabolism
Streptomyces chemistry
Streptomyces metabolism
Transaminases antagonists & inhibitors
Transaminases genetics
Bacterial Proteins metabolism
Diketopiperazines chemistry
Formycins biosynthesis
Pyridoxal Phosphate chemistry
Pyridoxamine analogs & derivatives
Transaminases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1364-548X
- Volume :
- 55
- Issue :
- 96
- Database :
- MEDLINE
- Journal :
- Chemical communications (Cambridge, England)
- Publication Type :
- Academic Journal
- Accession number :
- 31730149
- Full Text :
- https://doi.org/10.1039/c9cc06975e