Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.4.2.12: nicotinamide phosphoribosyltransferase

This is an abbreviated version!
For detailed information about nicotinamide phosphoribosyltransferase, go to the full flat file.

Word Map on EC 2.4.2.12

Reaction

nicotinamide D-ribonucleotide
+
diphosphate
=
nicotinamide
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

eNAMPT, extracellular nicotinamide phosphoribosyltrasferase, iNAMPT, Nam phosphoribosyltransferase, NAmPRTase, Nampt, Nampt/PBEF/Visfatin, Nampt/visfatin, NAMPTA, NAMPTB, NAPRT, nicotinamide mononucleotide pyrophosphorylase, nicotinamide mononucleotide synthetase, nicotinamide phosphoribosyl transferase, nicotinamide phosphoribosyltransferase, nicotinamide phosphoribosyltransferase/Visfatin, NMN pyrophosphorylase, NMN synthetase, NMPRTase, PBEF, phosphoribosyltransferase, nicotinamide, pre-B cell colony enhancing factor, pre-B cell colony enhancing factor(PBEF), pre-B cell colony-enhancing factor, pre-B cell colony-enhancing factor (PBEF), pre-B cell colony-enhancing factor 1, pre-B colony enhancing factor, pre-B-cell colony enhancing factor, pre-B-cell colony-enhancing factor, Visfatin

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.12 nicotinamide phosphoribosyltransferase

Crystallization

Crystallization on EC 2.4.2.12 - nicotinamide phosphoribosyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo enzyme, diffraction of third crystals at 2 A resolution at -174°C, crystals belong to space group P2(1) with unit-cell parameters a = 60.56 A, b = 106.40 A, c =82.78 A, beta = 96.50°, technique: 1 microlitre of 10 mg/ml protein solution to 1 microlitre reservoir solution (38% pentaerytritol propoxylate (5/4 PO/OH) and 200 mM KCl pH 9) one week at 4°C, generation of first crystals by hanging-drop vapour diffusion (Index HT screening kit), generation of second crystals by microseeding: reservoir solution contained crushed first crystals, generation of third crystals by Repeated Seeding Technique: reservoir solution contained crushed second crystals
crystal structures at up to 2.1 A resolution of NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. Crystals of the selenomethionyl free enzyme of human NMPRTase (F132M I151M double mutant) are grown with the sitting drop vapor diffusion method at 22°C. Crystals of wild-type human NMPRTase in complex with NMN are obtained at 22°C by sitting drop vapor diffusion
crystal structures of the enzyme in the free form and bound to nicotinamide and 5-phospho-alpha-D-ribose 1-diphosphate at the resolution of 2.0 A to 2.2 A are essentially identical to that of the complex with nicotinamide mononucleotide, except for some variations that can facilitate the substitution reaction by fixing the nucleophile and the leaving group for the requisite inversion of configuration at the C1’-carbon of the ribose ring. In the active site near the C1’-atom of the bound 5-phospho-alpha-D-ribose 1-diphosphate or nicotinamide mononucleotide, there is neither negatively charged group nor waterproof environment necessary to support the feasibility of a ribo-oxocarbocation intermediate inherent in the SN1 mechanism
crystallization of recombinant human NMPRTase in the free form, sitting-drop vapour-diffusion method, hanging-drop vapour-diffusion method, crystal quality is improved by successive use of the microseeding technique. The resultant crystals diffract to 2.0 A resolution. These crystals belongs to space group P2(1), with unit-cell parameters a = 60.56, b = 106.40, c = 82.78 A
crystal structures at up to 2.1 A resolution of NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. Crystals of wild-type murine NMPRTase free enzyme are obtained by sitting drop vapor diffusion at 4°C
hanging drop vapor diffusion method, crystallization of apoenzyme and complex with either nicotinamide mononucleotide or the NAmPRTase inhibitor FK-866