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Literature summary for 4.1.2.13 extracted from

  • Lorentzen, E.; Siebers, B.; Hensel, R.; Pohl, E.
    Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates (2005), Biochemistry, 44, 4222-4229.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of Y146F covalently bound to the carbinolamine intermediate of the substrate fructose 1,6-bisphosphate and noncovalently bound to the cyclic form of the substrate. The structures are determined at a resolution of 1.9 A and refined to crystallographic R factors of 0.148 and 0.149, respectively. The crystal structure of the W144E/Y146F double-mutant substrate complex represents the first example where the cyclic form of beta-fructose 1,6-bisphosphate is noncovalently bound to FBPA I Thermoproteus tenax

Protein Variants

Protein Variants Comment Organism
Y146F catalytically deficient mutant Thermoproteus tenax

Organism

Organism UniProt Comment Textmining
Thermoproteus tenax P58315
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Synonyms

Synonyms Comment Organism
FBPA I
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Thermoproteus tenax
fructose-1,6-bisphosphate aldolase
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Thermoproteus tenax