(1) Department of Biochemistry, University College of Wales, SY23 3DD Aberystwyth, Dyfed, Wales, UK;(2) Department of Physiology, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, Denmark
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.Abbreviations AFPA
4-amino 5-fluoropentanoic acid
- ALA
-aminolaevulinic acid
- DTT
dithiothreitol
- GSA
glutamate 1-semialdehyde
- PAL-P
pyridoxal 5-phosphate
- PAM-P
pyridoxamine 5-phosphate
- PCC
Paris Culture Collection