NAD+review1999

Enzymology of NAD+ synthesis.

Advances in enzymology and related areas of molecular biology

confidence

Key findings

Review of enzymes and pathways in NAD+ biosynthesis and salvage; no clinical or biological endpoints reported.

Sample size: N/A
Population: Not applicable (enzymology review)
Dosing: N/A
Duration: N/A
Route: N/A
Blinding: not_reported
Controls: not_reported
Drug class: coenzyme

Full abstract

Beyond its role as an essential coenzyme in numerous oxidoreductase reactions as well as respiration, there is growing recognition that NAD+ fulfills many other vital regulatory functions both as a substrate and as an allosteric effector. This review describes the enzymes involved in pyridine nucleotide metabolism, starting with a detailed consideration of the anaerobic and aerobic pathways leading to quinolinate, a key precursor of NAD+. Conversion of quinolinate and 5'-phosphoribosyl-1'-pyrophosphate to NAD+ and diphosphate by phosphoribosyltransferase is then explored before proceeding to a discussion the molecular and kinetic properties of NMN adenylytransferase. The salient features of NAD+ synthetase as well as NAD+ kinase are likewise presented. The remainder of the review encompasses the metabolic steps devoted to (a) the salvaging of various niacin derivatives, including the roles played by NAD+ and NADH pyrophosphatases, nicotinamide deamidase, and NMN deamidase, and (b) utilization of niacins by nicotinate phosphoribosyltransferase and nicotinamide phosphoribosyltransferase.

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