Abstract
γ-Aminobutyric acid-α-ketoglutarate transaminase from pig brain is irreversibly inactivated by 4-amino-5-halopentanoic acids. Protection from inactivation by the natural substrates, the pH dependence of inactivation and the incorporation of 1.7 moles of radioactive inhibitor per mole of enzyme from (S)-[U-14C]-4-amino-5-chloropentanoic acid suggest a covalent adduct at the active site of the enzyme. A mechanism-based inactivation is proposed.
Original language | English (US) |
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Pages (from-to) | 250-255 |
Number of pages | 6 |
Journal | Topics in Catalysis |
Volume | 95 |
Issue number | 1 |
DOIs | |
State | Published - 1980 |
Keywords
- GABA
- GABA-T
- GAD
- NADP
- NADP
- PLP
- Pyr in Scheme 1 represents the substituted pyridine nucleus in PLP
- SSADH
- glutamate decarboxylase E.C. 4.1.1.14
- nicotinamide adenosine triphosphate
- oxidoreductase E.C. 1.2.1.16
- pyridoxal phosphate
- succinic semialdehyde
- α-KG
- α-ketoglutaric acid
- γ-aminobutyric acid
- γ-aminobutyric acid-α-ketoglutarate transaminase E.C. 2.6.1.19
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
- Biochemistry
- Biophysics
- Molecular Biology