Abstract
Glutamate 1-semialdehyde aminotransferase has been separated from metabolically related activities by gel filtration and affinity chromatography. The enzyme was inhibited by gabaculin, 4-amino 5-fluoropentanoic acid and pyridoxal 5-phosphate and stimulated by pyridoxamine 5-phosphate. The activity of enzyme recovered by elution after electrophoresis in non-denaturing polyacrylamide gels was wholly dependent on pyridoxamine 5-phosphate. A mechanism for the enzyme-catalysed reaction based on these observations is discussed.
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Abbreviations
- AFPA:
-
4-amino 5-fluoropentanoic acid
- ALA:
-
δ-aminolaevulinic acid
- DTT:
-
dithiothreitol
- GSA:
-
glutamate 1-semialdehyde
- PAL-P:
-
pyridoxal 5-phosphate
- PAM-P:
-
pyridoxamine 5-phosphate
- PCC:
-
Paris Culture Collection
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Bull, A.D., Breu, V., Kannangara, C.G. et al. Cyanobacterial glutamate 1-semialdehyde aminotransferase: requirement for pyridoxamine phosphate. Arch. Microbiol. 154, 56–59 (1990). https://doi.org/10.1007/BF00249178
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DOI: https://doi.org/10.1007/BF00249178