2003
DOI: 10.1074/jbc.m212394200
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Interaction of Tl+ with Product Complexes of Fructose-1,6-bisphosphatase

Abstract: Fructose-1,6-bisphosphatase requires divalent cations (Mg 2؉ , Mn 2؉ , or Zn 2؉ ) for catalysis, but a diverse set of monovalent cations (K ؉ , Tl ؉ , Rb ؉ , or NH 4 ؉ ) will further enhance enzyme activity. Here, the interaction of Tl ؉ with fructose-1,6-bisphosphatase is explored under conditions that support catalysis. On the basis of initial velocity kinetics, Tl ؉ enhances catalysis by 20% with a K a of 1.3 mM and a Hill coefficient near unity. Crystal structures of enzyme complexes with Mg 2؉ , Tl ؉ , an… Show more

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Cited by 13 publications
(24 citation statements)
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“…Nonetheless, the geometric relationship between P i and F6P ( Fig. 2A) is consistent with an associative reaction mechanism, the details of which have been presented elsewhere (40); Asp 74 (the pK a of which is raised by the proximity of Glu 98 ) abstracts a proton from a water molecule coordinated to the Mg 2ϩ at site 2 or site 3. The resulting Mg 2ϩ -coordinated hydroxide anion in turn abstracts the proton from a second water molecule (the attacking nucleophile) that bridges the magnesium cations at sites 2 and 3.…”
Section: Discussionmentioning
confidence: 57%
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“…Nonetheless, the geometric relationship between P i and F6P ( Fig. 2A) is consistent with an associative reaction mechanism, the details of which have been presented elsewhere (40); Asp 74 (the pK a of which is raised by the proximity of Glu 98 ) abstracts a proton from a water molecule coordinated to the Mg 2ϩ at site 2 or site 3. The resulting Mg 2ϩ -coordinated hydroxide anion in turn abstracts the proton from a second water molecule (the attacking nucleophile) that bridges the magnesium cations at sites 2 and 3.…”
Section: Discussionmentioning
confidence: 57%
“…Control Complex (PDB: 1NUY)-Aside from its substantially higher resolution (Table I), the control complex is essentially identical to the Mg 2ϩ product complex of Choe et al (29,30,40). Orthophosphate is clearly at the active site, and Mg 2ϩ occupies sites 1, 2, and 3 (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…Fluorescence from a tryptophan reporter group at position 57 is consistent with the conformational states for loop 52Ϫ72, observed in crystal structures (20,21). Presumably, the engaged, disengaged, and disordered conformations of loop 52Ϫ72 are possible in both the R-and T-states of FBPase, but only the engaged and disordered conformers of the R-state, and the disengaged conformer of the T-state, have been reported in crystalline complexes (17,18,22,23).A recent report (24) in the literature identifies a new inhibitor site on FBPase, distinct from the active and the AMPbinding sites. The new family of anilinoquinazoline inhibitors was discovered by a search for potential drugs in the treatment of non-insulin-dependent diabetes.…”
mentioning
confidence: 99%