L-Lysine: 2-oxoglutarate 6-aminotransferase. Subunit structure composed of non-identical polypeptides and pyridoxal 5'-phosphate-binding subunit.
L-Lysine:2-oxoglutarate 6-aminotransferase from Flavobacterium lutescence (= Achromobacter liquidum) has been shown to be composed of one each of four non-identical subunits, A, B1, B2, and C. The subunits were isolated by gel filtration, and DEAE-cellulose chromatography in the presence of 8 M urea. Their molecular weights were determined by ultracentrifugation, gel electrophoresis and gel filtration: subunit A 24,000; B1 28,000; B2 28,000; C 45,000. These subunits were all different in amino acid composition. Of the two molecules of bound pyridoxal 5'-phosphate, the one which absorbs at 415 nm is bound to subunit B2 and participates in the catalytic action of the enzyme.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D005417:Flavobacterium / Q000201:enzymology*; D051306:L-Lysine 6-Transaminase; D008239:Lysine / Q000302:isolation & purification / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D000637:Transaminases / Q000302:isolation & purification / Q000378:metabolism
D000596:Amino Acids; D046911:Macromolecular Substances; D011732:Pyridoxal Phosphate; D000637:Transaminases; D051306:L-Lysine 6-Transaminase; D008239:Lysine