http://purl.uniprot.org/citations/3753653 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3753653 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3753653 | http://www.w3.org/2000/01/rdf-schema#comment | "GTP cyclohydrolase I from human liver and Escherichia coli is competitively inhibited by 8-aminoguanosine triphosphate with a dissociation constant (Ki) of 0.25 mumol/l. 8-Aminoguanosine triphosphate, prepared from GTP and hydroxylamine-O-sulfonic acid, was coupled to Sepharose 4B and used as an affinity adsorbent for a 309-fold purification of GTP cyclohydrolase I from human liver. GTP cyclohydrolase I from human liver is a relatively heat-stable enzyme with a half-life of 2 min at 80 degrees C, an isoelectric point (pI) of about 5.6, and a Km for GTP of 31 mumol/l. Addition of KCl (0.3 mol/l) increased the Km to 153 mumol/l. No cofactors were required for activity. L-erythro-5,6,7,8-Tetrahydrobiopterin, L-erythro-7,8-dihydrobiopterin, L-sepiapterin and 8-aminoguanosine triphosphate were strong inhibitors."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.org/dc/terms/identifier | "doi:10.1016/0304-4165(86)90115-7"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.org/dc/terms/identifier | "doi:10.1016/0304-4165(86)90115-7"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/author | "Blau N."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/author | "Blau N."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/author | "Niederwieser A."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/author | "Niederwieser A."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/name | "Biochim. Biophys. Acta"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/name | "Biochim. Biophys. Acta"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/pages | "26-31"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/pages | "26-31"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/title | "The application of 8-aminoguanosine triphosphate, a new inhibitor of GTP cyclohydrolase I, to the purification of the enzyme from human liver."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/title | "The application of 8-aminoguanosine triphosphate, a new inhibitor of GTP cyclohydrolase I, to the purification of the enzyme from human liver."xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/volume | "880"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://purl.uniprot.org/core/volume | "880"xsd:string |
http://purl.uniprot.org/citations/3753653 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3753653 |
http://purl.uniprot.org/citations/3753653 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3753653 |
http://purl.uniprot.org/citations/3753653 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3753653 |
http://purl.uniprot.org/citations/3753653 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3753653 |
http://purl.uniprot.org/uniprot/P30793 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3753653 |
http://purl.uniprot.org/uniprot/P30793#attribution-4A4972F0CDBB47A6B6DD4345728974FF | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/3753653 |