formycin and pyridoxamine-phosphate

formycin has been researched along with pyridoxamine-phosphate* in 1 studies

Other Studies

1 other study(ies) available for formycin and pyridoxamine-phosphate

Article	Year
PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis. Chemical communications (Cambridge, England), 2019, Nov-28, Volume: 55, Issue:96 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. Topics: Bacterial Proteins; Biocatalysis; Catalytic Domain; Cycloserine; Diketopiperazines; Formycins; Hydrogen-Ion Concentration; Pyridoxal Phosphate; Pyridoxamine; Streptomyces; Transaminases	2019

Article

Year

PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis.

Chemical communications (Cambridge, England), 2019, Nov-28, Volume: 55, Issue:96

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.

Topics: Bacterial Proteins; Biocatalysis; Catalytic Domain; Cycloserine; Diketopiperazines; Formycins; Hydrogen-Ion Concentration; Pyridoxal Phosphate; Pyridoxamine; Streptomyces; Transaminases

2019