Pages that link to "Q52533340"

The following pages link to Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism. (Q52533340):

Displaying 9 items.

• Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima (Q27622016) (← links)
• Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family (Q27639101) (← links)
• Replacement of a Phenylalanine by a Tyrosine in the Active Site Confers Fructose-6-phosphate Aldolase Activity to the Transaldolase of Escherichia coli and Human Origin (Q27651458) (← links)
• Conservation of structure and mechanism within the transaldolase enzyme family (Q27676515) (← links)
• Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases (Q31713236) (← links)
• The transaldolase family: new synthetic opportunities from an ancient enzyme scaffold (Q37875830) (← links)
• Transaldolase of Methanocaldococcus jannaschii (Q42652576) (← links)
• Human glutathione transferase A1-1 demonstrates both half-of-the-sites and all-of-the-sites reactivity (Q43684816) (← links)
• Transaldolase B: trapping of Schiff base intermediate between dihydroxyacetone and epsilon-amino group of active-site lysine residue by borohydride reduction (Q44206241) (← links)