http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID398437
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | NAT, N-acetyltransferase, of N-acetylglutamate synthase. This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696. |
| title | NAT |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18771910 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20812677 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16789063 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 15.