We identified an OsGlnB gene that encoded a bacterial PII-like protein in rice. Yeast two-hybrid analysis showed that an OsGlnB gene product interacted with N-acetylglutamate kinase 1 (OsNAGK1) and PII-like protein (OsGlnB) itself in rice. In cyanobacteria, NAGK is a key enzyme in ...
Interaction of N-acetylglutamate kinase with a PII-like protein in rice. PII protein in bacteria is a sensor for 2-oxoglutarate and a transmitter for glutamine signaling. We identified an OsGlnB gene that encoded a bacterial PII... S Kenjiro,H Toshihiko,K Toru,... - 《Plant & Cell ...
We identified amino acids responsible for binding of arginine to vertebrate-like NAGS based on the information from three dimensional structure ofThermotoga maritimaN-acetylglutamate kinase (NAGK) protein liganded with L-arginine [72] and mutagenesis studies in NAGS fromP. aeruginosaandE. coli[67,73...
Fita, V. Rubio, Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase, PLoS ONE 7 (2012) e34734.de Cima S, Gil-Ortiz F, Crabeel M, Fita I, Rubio V. Insight on an arginine synthesis metabolon from the tetrameric structure of yeast ...
Each monomer has two domains: an amino acid kinase (AAK) domain with an AAK-like fold but lacking kinase activity and an N-acetyltransferase (NAT) domain homologous to other GCN5-related transferases. Binding of L-arginine to the AAK domain induces a global conformational change that increases...
We have reported that l-glutamate transport by crayfish central nerve fibers resides in glia and axons (Kane et al., 2000), possesses chemical characteristics like those of glutamate transport systems of vertebrate and invertebrate neural tissues (Kane et al., 2000), and contributes to formation ...