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Literature summary for 2.4.2.19 extracted from

  • Youn, H.S.; Kim, T.G.; Kim, M.K.; Kang, G.B.; Kang, J.Y.; Lee, J.G.; An, J.Y.; Park, K.R.; Lee, Y.; Im, Y.J.; Lee, J.H.; Eom, S.H.
    Structural insights into the quaternary catalytic mechanism of hexameric human quinolinate phosphoribosyltransferase, a key enzyme in de novo NAD biosynthesis (2016), Sci. Rep., 6, 19681.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
apoenzyme and in complex with quinolinic acid or nicotinic acid mononucleotide, hanging drop vapor diffusion method, using Homo sapiens

Protein Variants

Protein Variants Comment Organism
R161A the mutation abolishes substrate binding and enzyme activity with a 20% capacity of wild type enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
quinolinic acid + 5-phospho-alpha-D-ribose 1-diphosphate Homo sapiens
-
nicotinic acid mononucleotide + diphosphate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q15274
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
quinolinic acid + 5-phospho-alpha-D-ribose 1-diphosphate
-
Homo sapiens nicotinic acid mononucleotide + diphosphate + CO2
-
?

Subunits

Subunits Comment Organism
hexamer x-ray crystallography Homo sapiens

Synonyms

Synonyms Comment Organism
QPRT
-
Homo sapiens
quinolinate phosphoribosyltransferase
-
Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
83.6
-
melting temperature Homo sapiens

General Information

General Information Comment Organism
physiological function the enzyme is essential for maintaining the homeostasis of quinolinic acid in the brain Homo sapiens