2YCE
| Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate. | Descriptor: | D-MANNITOL-1,6-DIPHOSPHATE, FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1 | Authors: | Lorentzen, E, Siebers, B, Hensel, R, Pohl, E. | Deposit date: | 2011-03-14 | Release date: | 2011-04-27 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.93 Å) | Cite: | Mechanism of the Schiff Base Forming Fructose-1,6-Bisphosphate Aldolase: Structural Analysis of Reaction Intermediates. Biochemistry, 44, 2005
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1W8S
| The mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural analysis of reaction intermediates | Descriptor: | 1,6-di-O-phosphono-beta-D-fructofuranose, FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS I | Authors: | Lorentzen, E, Hensel, R, Siebers, B, Pohl, E. | Deposit date: | 2004-09-27 | Release date: | 2005-03-23 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates. Biochemistry, 44, 2005
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