This is the N-terminal domain found in Nicotinamide phosphoribosyltransferase (NAMPT) present in Homo sapiens. NAMPT captures nicotinamide (NAM) and replenishes the nicotinamide adenine dinucleotide (NAD+) pool during ADP-ribosylation and transferase reactions [].
Nicotinamide phosphoribosyl transferase (NAMPT) catalyses the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD [, ]. NAMPT is also known as pre-B cell colony-enhancing factor (PBEF) or visfatin.
Nicotinate phosphoribosyltransferase () is the rate-limiting enzyme that catalyses the first reaction in the NAD salvage synthesis []. Members in this family can be split into two further subfamilies represented in and . Members in have a different (longer) spacing of several key motifs and have an additional C-terminal domain of up to 100 residues. However, one argument suggesting that this family represents the same enzyme is that no species has a member of both subfamilies. Another is that the gene encoding this protein is located near other NAD salvage biosynthesis genes in Nostoc and in at least four different Gram-positive bacteria.Nicotinamide phosphoribosyl transferase (NAMPT) catalyses the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD [, ]. NAMPT is also known as pre-B cell colony-enhancing factor (PBEF) or visfatin.
