Brain 4-aminobutyrate aminotransferase: Isolation and sequence of a cDNA encoding the enzyme

Oh Shin Kwon, Joohong Park, Jorge E. Churchich

Research output: Contribution to journalArticlepeer-review

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Abstract

4-Aminobutyrate aminotransferase is a key enzyme of the 4-aminobutyric acid shunt. It is responsible for the conversion of the neurotransmitter 4-aminobutyrate to succinic semialdehyde. By using oligonucleotide probes based on partial amino acid sequence data for the pig brain enzyme, several overlapping cDNA clones of 2.0-2.2 kilobases in length have been isolated. The largest cDNA clone was selected for sequence analysis. The amino acid sequence predicted from the cDNA sequence shows that the precursor of 4-aminobutyrate aminotransferase consists of the mature enzyme of 473 amino acid residues and an amino-terminal segment of 27 amino acids attributed to the signal peptide. The cofactor pyridoxal-5-P is bound to lysine residue 330 of the deduced amino acid sequence of the mature enzyme.

Original languageEnglish
Pages (from-to)7215-7216
Number of pages2
JournalJournal of Biological Chemistry
Volume267
Issue number11
StatePublished - 15 Apr 1992

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