PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1681900-0 1991 Identification of the ATP binding sites of the carbamyl phosphate synthetase domain of the Syrian hamster multifunctional protein CAD by affinity labeling with 5"-[p-(fluorosulfonyl)benzoyl]adenosine. Adenosine Triphosphate 22-25 CAD protein Mesocricetus auratus 130-133 1681900-3 1991 ATP protected CAD against inactivation by FSBA whereas the presence of the allosteric effectors UTP and PRPP afforded little protection, which suggests that the ATP binding sites were specifically labeled. Adenosine Triphosphate 0-3 CAD protein Mesocricetus auratus 14-17 1681900-8 1991 Amino acid sequencing of the principal peaks resulting from tryptic digests of FSBA-modified CAD located the sites of FSBA modification in regions that exhibit high homology to ATP binding sites of other known proteins. Adenosine Triphosphate 177-180 CAD protein Mesocricetus auratus 93-96 1681900-9 1991 Thus CAD has two ATP binding sites, one in each of the two highly homologous halves of the carbamyl phosphate domain which catalyze distinct ATP-dependent partial reactions in carbamyl phosphate synthesis. Adenosine Triphosphate 17-20 CAD protein Mesocricetus auratus 5-8 1681900-9 1991 Thus CAD has two ATP binding sites, one in each of the two highly homologous halves of the carbamyl phosphate domain which catalyze distinct ATP-dependent partial reactions in carbamyl phosphate synthesis. Adenosine Triphosphate 141-144 CAD protein Mesocricetus auratus 5-8