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Literature summary for 2.6.1.19 extracted from

  • Clift, M.D.; Ji, H.; Deniau, G.P.; OHagan, D.; Silverman, R.B.
    Enantiomers of 4-amino-3-fluorobutanoic acid as substrates for gamma-aminobutyric acid aminotransferase. Conformational probes for GABA binding (2007), Biochemistry, 46, 13819-13828.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
(R,S)-4-amino-3-fluorobutanoic acid the (R)-enantiomer inhibits the transamination of gamma-aminobutanoic acid 10 times more effectively than the (S)-enantiomer. On binding of free 4-amino-3-fluorobutanoic acid to enzyme the optimal conformation places the C-NH3 + and C-F bonds gauche in the (R)-enantiomer but anti in the (S)-enantiomer Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.045
-
(R,S)-4-amino-3-fluorobutanoic acid pH 8.5 Sus scrofa
0.059
-
(R)-4-amino-3-fluorobutanoic acid pH 8.5 Sus scrofa
2.6
-
gamma-aminobutanoic acid pH 8.5 Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa P80147
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.89
-
pH 8.5 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-4-amino-3-fluorobutanoic acid
-
Sus scrofa 4-aminobut-2-enoic acid + HF
-
?
(R,S)-4-amino-3-fluorobutanoic acid neither enantiomer is a substrate for transamination. The rate of elimination of HF from the (R)-enantiomer is at least 10 times greater than that for the (S)-enantiomer Sus scrofa 4-aminobut-2-enoic acid + HF
-
?
gamma-aminobutyric acid
-
Sus scrofa ?
-
?