Irreversible inactivation of pig brain γ-aminobutyric acid-α-ketoglutarate transaminase by 4-amino-5-halopentanoic acids

R. B. Silverman; M. A. Levy

doi:10.1016/0006-291X(80)90731-7

Irreversible inactivation of pig brain γ-aminobutyric acid-α-ketoglutarate transaminase by 4-amino-5-halopentanoic acids

R. B. Silverman^*, M. A. Levy

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

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)
Pages (from-to)	250-255
Number of pages	6
Journal	Topics in Catalysis
Volume	95
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(80)90731-7
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

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title = "Irreversible inactivation of pig brain γ-aminobutyric acid-α-ketoglutarate transaminase by 4-amino-5-halopentanoic acids",

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.",

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author = "Silverman, {R. B.} and Levy, {M. A.}",

year = "1980",

doi = "10.1016/0006-291X(80)90731-7",

language = "English (US)",

volume = "95",

pages = "250--255",

journal = "Topics in Catalysis",

number = "1",

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T1 - Irreversible inactivation of pig brain γ-aminobutyric acid-α-ketoglutarate transaminase by 4-amino-5-halopentanoic acids

AU - Silverman, R. B.

AU - Levy, M. A.

PY - 1980

Y1 - 1980

N2 - 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.

AB - 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.

KW - GABA

KW - GABA-T

KW - GAD

KW - NADP

KW - PLP

KW - Pyr in Scheme 1 represents the substituted pyridine nucleus in PLP

KW - SSADH

KW - glutamate decarboxylase E.C. 4.1.1.14

KW - nicotinamide adenosine triphosphate

KW - oxidoreductase E.C. 1.2.1.16

KW - pyridoxal phosphate

KW - succinic semialdehyde

KW - α-KG

KW - α-ketoglutaric acid

KW - γ-aminobutyric acid

KW - γ-aminobutyric acid-α-ketoglutarate transaminase E.C. 2.6.1.19

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ER -

Irreversible inactivation of pig brain γ-aminobutyric acid-α-ketoglutarate transaminase by 4-amino-5-halopentanoic acids

Abstract

Keywords

ASJC Scopus subject areas

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