Literature summary for 4.1.2.13 extracted from

St-Jean, M.; Lafrance-Vanasse, J.; Liotard, B.; Sygusch, J.
High resolution reaction intermediates of rabbit muscle fructose-1,6-bisphosphate aldolase: substrate cleavage and induced fit (2005), J. Biol. Chem., 280, 27262-27270.

Crystallization (Commentary)

Crystallization (Comment)	Organism
recombinant enzyme, vapour diffusion method. Crystal structures are determined to 1.8 Å resolution of fructose-1,6-bis(phosphate) aldolase trapped in complex with its substrate and a competitive inhibitor, mannitol-1,6-bis(phosphate). The enzyme substrate complex corresponds to the postulated Schiff base intermediate and has reaction geometry consistent with incipient C3-C4 bond cleavage catalyzed by Glu187, which is adjacent to the Schiff base-forming Lys229	Oryctolagus cuniculus

Crystallization (Comment)

Organism

recombinant enzyme, vapour diffusion method. Crystal structures are determined to 1.8 Å resolution of fructose-1,6-bis(phosphate) aldolase trapped in complex with its substrate and a competitive inhibitor, mannitol-1,6-bis(phosphate). The enzyme substrate complex corresponds to the postulated Schiff base intermediate and has reaction geometry consistent with incipient C3-C4 bond cleavage catalyzed by Glu187, which is adjacent to the Schiff base-forming Lys229

Oryctolagus cuniculus

Inhibitors

Inhibitors	Comment	Organism	Structure
mannitol-1,6-bis(phosphate)	competitive	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P00883	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Oryctolagus cuniculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Oryctolagus cuniculus	-

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Release 2023.1 (January 2023)