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Cyanobacterial glutamate 1-semialdehyde aminotransferase: requirement for pyridoxamine phosphate
Authors:Alan D Bull  Volker Breu  C Gamini Kannangara  Lyndon J Rogers  Arnold J Smith
Institution:(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 delta-aminolaevulinic acid - DTT dithiothreitol - GSA glutamate 1-semialdehyde - PAL-P pyridoxal 5-phosphate - PAM-P pyridoxamine 5-phosphate - PCC Paris Culture Collection
Keywords:Aminolaevulinic acid  Aminotransferase  Chlorophyll  Cyanobacterium  Gabaculin  Glutamate semialdehyde  Pyridoxal  Pyridoxamine  Synechococcus  Tetrapyrrole
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