Protein Family Models

Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide [1,2]. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The N-terminal domain has an alpha/beta hammerhead fold. [1]. 9016724. A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. Eads JC, Ozturk D, Wexler TB, Grubmeyer C, Sacchettini JC;. Structure 1997;5:47-58. [2]. 8561507. The sequencing expression, purification, and steady-state kinetic analysis of quinolinate phosphoribosyl transferase from Escherichia coli. Bhatia R, Calvo KC;. Arch Biochem Biophys 1996;325:270-278. [3]. 26042198. Crystal structure of human nicotinic acid phosphoribosyltransferase. Marletta AS, Massarotti A, Orsomando G, Magni G, Rizzi M, Garavaglia S;. FEBS Open Bio. 2015;5:419-428. (from Pfam)

Date:

2024-10-16

nicotinate phosphoribosyltransferase (NAPRTase) catalyzes the first and rate limiting step of the NAD salvage pathway, the formation of nicotinic acid mononucleotide (NAMN) and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid

Date:

2024-11-19

Catalyzes the formation of 5-phospho-alpha-D-ribose 1-diphosphate and nicotinate from nicotinate D-ribonucleotide and diphosphate

Date:

2020-10-26