BRENDA - Enzyme Database show

Structure and reaction mechanism of human nicotinamide phosphoribosyltransferase

Takahashi, R.; Nakamura, S.; Nakazawa, T.; Minoura, K.; Yoshida, T.; Nishi, Y.; Kobayashi, Y.; Ohkubo, T.; J. Biochem. 147, 95-107 (2010)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
2.4.2.12
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
Homo sapiens
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.2.12
Homo sapiens
P43490
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.2.12
nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate
reaction is reversible as dictated by the equilibrium constant K, [NMN][PPi]/([NM][PRPP]) of 0.14, which agrees well with the ratio of second-order rate constants for forward and backward reactions, K of0.16
704364
Homo sapiens
nicotinamide D-ribonucleotide + diphosphate
-
-
-
r
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.4.2.12
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
Homo sapiens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.2.12
nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate
reaction is reversible as dictated by the equilibrium constant K, [NMN][PPi]/([NM][PRPP]) of 0.14, which agrees well with the ratio of second-order rate constants for forward and backward reactions, K of0.16
704364
Homo sapiens
nicotinamide D-ribonucleotide + diphosphate
-
-
-
r