|
type |
Journal Article |
authors |
Kwon, O. S.; Park, J.; Churchich, J. E. |
title |
Brain 4-aminobutyrate aminotransferase. Isolation and sequence of a cDNA encoding the enzyme |
journal |
J Biol Chem |
Activity |
2.6.1.19 |
sel |
selected |
ui |
1559966 |
year |
(1992) |
volume |
267 |
number |
11 |
pages |
7215-6 |
| |
keywords |
4-Aminobutyrate Transaminase/*genetics/isolation & purification/metabolism |
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. |
last changed |
2009/04/30 10:27 |
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