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Synechococcus mutants resistant to an enamine mechanism inhibitor of glutamate‐1‐semialdehyde aminotransferase
Author(s) -
Bishop Konrad,
Gough Kevin,
Mahoney Sonia,
Smith Arnold,
Rogers Lyndon
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00465-2
Subject(s) - mutant , biochemistry , amino acid , glutamate synthase , enzyme , enamine , chemistry , synechococcus , biology , gene , microbiology and biotechnology , cyanobacteria , bacteria , glutamine synthetase , genetics , glutamine , catalysis
An enamine mechanism‐based inactivator of mammalian δ‐aminobutyric acid aminotransferase, 4‐amino 5‐fluoropentanoic acid is a potent inhibitor of cell growth and pigment formation in the cyanobacterium Synechococcus PCC 6301. It was demonstrated that 4‐amino 5‐fluoropentanoic acid inhibits the aminolaevulinate synthesis at glutamate 1‐semialdehyde aminotransferase and that in the mutant obtained by exposing cells to 40 μM 4‐amino 5‐fluoropentanoic acid, this enzyme was insensitive to the inhibitor. The specific activity of glutamate 1‐semialdehyde aminotransferase in cell extracts was lower in the mutant, although the cell growth rate was unaffected. The decrease in sensitivity to 4‐amino 5‐fluoropentanoic acid in the mutant is due to a structural gene mutation, a single base change in the hem L gene resulting in a S162T substitution in the gene product.