Purification and expression of a processing protease on beta-alanine-oxoglutarate aminotransferase from rat liver mitochondria
- Resource Type
- Authors
- Masahisa Horiuchi; Shigeko Fujimoto Sakata; Hideyuki Tachibana; Koichi Matsuda; Masataka Mori; Nanaya Tamaki; Tomoko Ohyama
- Source
- FEBS letters. 572(1-3)
- Subject
- Male
Swine
medicine.medical_treatment
Protein subunit
Molecular Sequence Data
Biophysics
β-Alanine aminotransferase
Peptide
Mitochondria, Liver
Carbamoyl-phosphate synthetase
Biology
Transfection
Biochemistry
β-Alanine
Mice
Structural Biology
Endopeptidases
Genetics
medicine
Animals
Humans
4-Aminobutyrate aminotransferase
Amino Acid Sequence
Rats, Wistar
Molecular Biology
Peptide sequence
Conserved Sequence
Transaminases
chemistry.chemical_classification
Alanine
Expression vector
Protease
Molecular mass
Sequence Homology, Amino Acid
Alanine Transaminase
Cell Biology
3T3 Cells
Molecular biology
Recombinant Proteins
Rats
chemistry
Mitochondrial processing peptidase
Oxoglutarate dehydrogenase complex
Sequence Alignment
4-Aminobutyrate
- Language
- ISSN
- 0014-5793
GABA(arrow beta)AlaAT convertase is an endopep- tidase that processes brain-type 4-aminobutyrate aminotransferase (GABA AT; EC 2.6.1.19) to liver-type b-alanine-oxoglutarate aminotransferase (b-AlaAT I) in rats. Its molecular mass was 180 kDa as determined by gel filtration. A subunit molecular mass of 97 652 Da was measured using MALDI-TOF MS. The N-terminal sequence of the purified GABA(arrow beta)AlaAT convertase was SRVEVSKVLILGSGGLSIGQAGEFDYSGS- QAV- and was identical to residues 418-449 of carbamoyl- phosphate synthetase I (CPS I; EC 1.2.1.27) purified from rat liver. The subunit molecular mass and the N-terminal amino acid sequence suggested that GABA(arrow beta)AlaAT convertase was the 418-1305 peptide of CPS I. An expression vector containing the coding region of the 418-1305 peptide of rat CPS I was transfected into NIH3T3 cells and the extract of the cells showed GABA(arrow beta)AlaAT convertase activity. 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.