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4-aminobutyrate—pyruvate transaminase
Class of enzymes
Class of enzymes
| Field | Value |
|---|---|
| Name | 4-aminobutyrate---pyruvate transaminase |
| EC_number | 2.6.1.96 |
4-aminobutyrate---pyruvate transaminase (aminobutyrate aminotransferase, gamma-aminobutyrate aminotransaminase, gamma-aminobutyrate transaminase, gamma-aminobutyric acid aminotransferase, gamma-aminobutyric acid pyruvate transaminase, gamma-aminobutyric acid transaminase, gamma-aminobutyric transaminase, 4-aminobutyrate aminotransferase, 4-aminobutyric acid aminotransferase, aminobutyrate transaminase, GABA aminotransferase, GABA transaminase, GABA transferase, POP2 (gene)) is an enzyme with systematic name 4-aminobutanoate:pyruvate aminotransferase. This enzyme is a type of GABA transaminase, which degrades the neurotransmitter GABA. The enzyme catalyses the following chemical reaction
: (1) 4-aminobutanoate + pyruvate \rightleftharpoons succinate semialdehyde + L-alanine : (2) 4-aminobutanoate + glyoxylate \rightleftharpoons succinate semialdehyde + glycine
This enzyme requires pyridoxal 5'-phosphate.
Clinical significance
Phenylethylidenehydrazine, the active metabolite of phenelzine, inhibits gamma-aminobutyric acid transaminase and subsequently increases GABA concentrations in the central nervous system. This may contribute to the notable anxiolytic effects of phenelzine.
References
References
- (1999). "Biochemical characterization of partially purified gaba:pyruvate transaminase from ''Nicotiana tabacum''". Phytochemistry.
- (July 2003). "Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene that controls GABA levels". Cell.
- (2009). "Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis gamma-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate". Journal of Experimental Botany.
- (2009). "Subcellular localization and expression of multiple tomato gamma-aminobutyrate transaminases that utilize both pyruvate and glyoxylate". Journal of Experimental Botany.
- (1994). "Amine Oxidases: Function and Dysfunction".
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