Statements in which the resource exists as a subject.
PredicateObject
rdf:type
biopax3:comment
FUNCTION: Involved in the catabolism of quinolinic acid (QA). CATALYTIC ACTIVITY: Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1- diphosphate. ENZYME REGULATION: Activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for QA (at 0.1 mM PRPP); KM=23 uM for QA (at 0.3 mM PRPP); Vmax=1.2 uM/min/mg enzyme (at 0.3 mM QA and 0.1 mM PRPP); Vmax=0.93 uM/min/mg enzyme (at 0.3 mM QA and 0.3 mM PRPP); PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D- ribonucleotide from quinolinate: step 1/1. SUBUNIT: Hexamer formed by 3 homodimers. SIMILARITY: Belongs to the nadC/modD family. GENE SYNONYMS:QPRT. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 297 AA; 30846 MW; E3199814DB9FA0D5 CRC64;
biopax3:xref
biopax3:displayName
NADC_HUMAN
biopax3:name
2.4.2.19, QAPRTase, QPRT, QPRTase, Quinolinate phosphoribosyltransferase [decarboxylating]
biopax3:organism
biopax3:sequence
MDAEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKSPGVLAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLFAKEVAPVPKIH
biopax3:standardName
Nicotinate-nucleotide pyrophosphorylase [carboxylating]