[Interaction of 4-aminobutyrate-transaminase from swine kidneys with 5'- and 6'-methyl derivatives of pyridoxal-5'-phosphate].
The study of interaction of 4-aminobutyrate transaminase with 5'- 6'-methyl derivates of PLP demonstrated that only the former was capable of forming a catalytically active holoenzyme possessing 0.37 activity of the native holoenzyme and a low affinity substrates. This compound interacts with the apoenzyme at a slower rate than does PLP; it has a reduced affinity towards apotransaminase (Km = 1.10(-4) M) and is replaced from the active site by native coenzyme. The other analog of pyridoxal-5'-phosphate forms a catalytically inactive complex with the apoenzyme; the other analog is not replaced from the active center by native coenzyme and non-competitively inhibits the reconstruction of apotransaminase (Ki = 2.10(-5) M).
D000612:4-Aminobutyrate Transaminase; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D007668:Kidney / Q000201:enzymology; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives*; D013552:Swine; D000637:Transaminases
D011732:Pyridoxal Phosphate; D000637:Transaminases; D000612:4-Aminobutyrate Transaminase
Vzaimodeĭstvie 4-aminobutirat-transaminazy iz pochek svin'i s 5'-i 6'metilproizvodnymi piridoksal-5'-fosfata