Article
Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine.
The Journal of biological chemistry - 2 Mar 2012
Veiga-da-Cunha Maria, Hadi Farah, Balligand Thomas, Stroobant Vincent, Van Schaftingen Emile
Abstract excerpt
The purpose of the present work was to identify the catalytic activity of AGXT2L1 and AGXT2L2, two closely related, putative pyridoxal-phosphate-dependent enzymes encoded by vertebrate genomes. The existence of bacterial homologues (40-50% identity with AGXT2L1 and AGXT2L2) forming bi- or tri-functional proteins with a putative kinase belonging to the family of aminoglycoside phosphotransferases suggested that...
Topics
- Animals
- Bacteria
- Bacterial Proteins
- Bipolar Disorder
- Ethanolamines
- Genome, Bacterial
- Genome, Human
- Humans
- Hydroxylysine
- Mutation
- Schizophrenia
