MJ0400 From Methanocaldococcus Jannaschii Exhibits fructose-1,6-bisphosphate Aldolase Activity

FEMS Microbiol Lett. 2008 Apr;281(1):36-41. doi: 10.1111/j.1574-6968.2008.01079.x.

Abstract

The central carbon metabolism is well investigated in bacteria, but this is not the case for archaea. MJ0400-His(6) from Methanocaldococcus jannaschii catalyzes the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate with a V(max) of 33 mU mg(-1) and a K(m) of 430 microM at 50 degrees C. MJ0400-His(6) is inhibited competitively by erythrose-4-phosphate with a K(i) of 380 microM and displays heat stability with a half-life of c. 1 h at 100 degrees C. Hence, MJ0400 is the second gene encoding for an FBP aldolase in M. jannaschii. Previously, MJ0400 was shown to act as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase. This indicates that MJ0400 is involved in both the carbon metabolism and the shikimate pathway in M. jannaschii.

MeSH terms

  • Carbon / metabolism
  • Cloning, Molecular
  • Dihydroxyacetone Phosphate
  • Enzyme Inhibitors / pharmacology
  • Enzyme Stability
  • Escherichia coli / genetics
  • Fructose-Bisphosphate Aldolase / genetics*
  • Fructose-Bisphosphate Aldolase / metabolism*
  • Gene Expression
  • Glyceraldehyde 3-Phosphate / metabolism
  • Hot Temperature
  • Kinetics
  • Methanococcales / enzymology*
  • Methanococcales / genetics*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Shikimic Acid / metabolism
  • Sugar Phosphates / pharmacology
  • Temperature

Substances

  • Enzyme Inhibitors
  • Recombinant Proteins
  • Sugar Phosphates
  • Glyceraldehyde 3-Phosphate
  • Shikimic Acid
  • Dihydroxyacetone Phosphate
  • erythrose 4-phosphate
  • Carbon
  • Fructose-Bisphosphate Aldolase