| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10803842 | Biochimie | 2012 | 10 Pages |
Abstract
⺠We characterized kinetically and structurally a recombinant human NaPRT. ⺠Metabolites of carbohydrate and lipid metabolism effect the enzyme activity. ⺠Structure prediction by homology modeling and docking studies have been performed. ⺠A detailed functional study through site-directed mutagenesis analysis is included.
Keywords
nicotinic acid mononucleotideIPTGRMSDNaPRTG3PDHAPPRPPNMN5-Phosphoribosyl-1-pyrophosphateSite-directed mutagenesisNicotinic acidQuinolinic acidisopropyl β-D-1-thiogalactopyranosidedihydroxyacetone phosphateNicotinamide ribosideEnzyme kineticsHomology modelingroot mean square deviationNAMNaMNnicotinamide phosphoribosyltransferasenicotinamide mononucleotidenicotinic acid adenine dinucleotideNicotinamideMolecular dockingglyceraldehyde 3-phosphate
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Authors
Lucia Galassi, Michele Di Stefano, Lucia Brunetti, Giuseppe Orsomando, Adolfo Amici, Silverio Ruggieri, Giulio Magni,