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4-aminobutyrate—pyruvate transaminase

Class of enzymes


Class of enzymes

FieldValue
Name4-aminobutyrate---pyruvate transaminase
EC_number2.6.1.96

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

  1. (1999). "Biochemical characterization of partially purified gaba:pyruvate transaminase from ''Nicotiana tabacum''". Phytochemistry.
  2. (July 2003). "Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene that controls GABA levels". Cell.
  3. (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.
  4. (2009). "Subcellular localization and expression of multiple tomato gamma-aminobutyrate transaminases that utilize both pyruvate and glyoxylate". Journal of Experimental Botany.
  5. (1994). "Amine Oxidases: Function and Dysfunction".
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