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TitleMechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates.
Journal, issue, pagesBiochemistry, Vol. 44, Page 4222-4229, Year 2005
Publish dateSep 27, 2004 (structure data deposition date)
AuthorsLorentzen, E. / Siebers, B. / Hensel, R. / Pohl, E.
External linksBiochemistry / PubMed:15766250
MethodsX-ray diffraction
Resolution1.85 - 1.93 Å
Structure data

PDB-1w8s:
The mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural analysis of reaction intermediates
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-2yce:
Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

Chemicals

ChemComp-FBP:
1,6-di-O-phosphono-beta-D-fructofuranose

ChemComp-HOH:
WATER

ChemComp-M2P:
D-MANNITOL-1,6-DIPHOSPHATE

Source
  • thermoproteus tenax (archaea)
KeywordsLYASE / ALDOLASE / FRUCTOSE 1 / 6-BISPHOSPHATE / TIM BARREL / GLYCOLYTIC / ARCHAEAL / CATALYTIC MECHANISM / REACTION INTERMEDIATE / GLYCOLYSIS

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