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.
MeSH terms
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Bacterial Proteins / antagonists & inhibitors
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Biocatalysis
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Catalytic Domain
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Cycloserine / chemistry
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Diketopiperazines / chemistry*
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Diketopiperazines / metabolism
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Formycins / biosynthesis*
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Formycins / chemistry
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Hydrogen-Ion Concentration
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Pyridoxal Phosphate / chemistry*
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Pyridoxamine / analogs & derivatives*
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Pyridoxamine / chemistry
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Pyridoxamine / metabolism
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Streptomyces / chemistry
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Streptomyces / metabolism
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Transaminases / antagonists & inhibitors
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Transaminases / genetics
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Transaminases / metabolism*
Substances
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Bacterial Proteins
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Diketopiperazines
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Formycins
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Pyridoxal Phosphate
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Pyridoxamine
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formycin
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Cycloserine
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Transaminases
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pyridoxamine phosphate