Rat liver mitochondria can synthesize nicotinamide adenine dinucleotide from nicotinamide mononucleotide and ATP via a putative matrix nicotinamide mononucleotide adenylyltransferase

Biochem Mol Biol Int. 1996 Feb;38(2):297-306.

Abstract

In order to gain some insight into the mechanism by which nicotinamide nucleotides localize in mitochondria, NMN was added to rat liver mitochondria, with NAD synthesis tested both enzymatically and by means of HPLC. Evidence is given that the mitochondrial matrix contains a specific NMN adenylyltransferase (E.C. 2.7.7.1.), inhibited by PPi, AMP and ADP-ribose. Some features of this enzyme, including the substrate, pH and temperature dependence were also investigated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / pharmacology
  • Adenosine Monophosphate / pharmacology
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Diphosphates
  • Hydrogen-Ion Concentration
  • Male
  • Mitochondria, Liver / enzymology
  • Mitochondria, Liver / metabolism*
  • NAD / biosynthesis*
  • NADP / biosynthesis
  • Nicotinamide Mononucleotide / metabolism*
  • Nicotinamide-Nucleotide Adenylyltransferase / metabolism*
  • Rats
  • Substrate Specificity

Substances

  • Diphosphates
  • NAD
  • Nicotinamide Mononucleotide
  • Adenosine Diphosphate Ribose
  • Adenosine Monophosphate
  • NADP
  • Adenosine Triphosphate
  • Nicotinamide-Nucleotide Adenylyltransferase