Does NADH play a central role in energy metabolism in Helicobacter pylori?

Trends Biochem Sci. 1998 Nov;23(11):412-3. doi: 10.1016/s0968-0004(98)01276-6.

Abstract

The complete genome sequence of Helicobacter pylori reveals an unusual NADH-quinone oxidoreductase (NDH-1 or Complex I) that might lack the NADH-binding domain. H. pylori also lacks various NADH-generating enzymes. What are the consequences for electron transfer to H. pylori NDH-1 and could NADPH be involved?

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Energy Metabolism / physiology*
  • Helicobacter pylori / physiology*
  • Molecular Sequence Data
  • NAD / physiology*
  • NAD(P)H Dehydrogenase (Quinone) / genetics
  • NAD(P)H Dehydrogenase (Quinone) / metabolism
  • Operon
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • NAD
  • NAD(P)H Dehydrogenase (Quinone)

Associated data

  • GENBANK/AE000631
  • GENBANK/P76489
  • GENBANK/Q46508
  • GENBANK/Q56223