Effects of pyridoxal phosphate N-oxide and 2'-hydroxy pyridoxal phosphate on L-aspartate beta-decarboxylase.
Pyridoxal phosphate N-oxide and 2'-hydroxypyridoxal phosphate served as the coenzyme for aspartate beta-decarboxylase (EC 4.1.1.12) from Pseudomonas dacunhae. Reconstituted enzymes with those pyridoxal phosphate analogues exhibited an absorption band near 370 nm. Close to 1 mole of vitamin B6 derivative is bound per minimal catalytic unit with high affinity. The decarboxylase, desulfinase, and transaminase activites of the both pyridoxal phosphate derivate-enzymes are relatively low. But the Km values for aspartate and cysteine sulfinate are not affected.
D001224:Aspartic Acid; D002262:Carboxy-Lyases; D003067:Coenzymes; D003653:Decarboxylation; D009589:Nitrogen Oxides; D011549:Pseudomonas / Q000201:enzymology; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives*; D013053:Spectrophotometry; D000637:Transaminases
D003067:Coenzymes; D009589:Nitrogen Oxides; D001224:Aspartic Acid; D011732:Pyridoxal Phosphate; D000637:Transaminases; D002262:Carboxy-Lyases