1995
DOI: 10.1016/0079-6107(95)00008-9
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Class I aldolases: Substrate specificity, mechanism, inhibitors and structural aspects

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Cited by 137 publications
(92 citation statements)
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“…The mechanism proposed here for transaldolase shares several features with the enzymatic mechanisms that have been proposed for F-1,6-P aldolase (Littlechild & Watson, 1993;Gefflaut et al, 1995). Residues corresponding to Asp 17 and Glu 96 are also found at the active site of F-1,6-P aldolases, Asp 33, and Glu 197, respectively.…”
Section: Proposed Mechanismsupporting
confidence: 75%
See 1 more Smart Citation
“…The mechanism proposed here for transaldolase shares several features with the enzymatic mechanisms that have been proposed for F-1,6-P aldolase (Littlechild & Watson, 1993;Gefflaut et al, 1995). Residues corresponding to Asp 17 and Glu 96 are also found at the active site of F-1,6-P aldolases, Asp 33, and Glu 197, respectively.…”
Section: Proposed Mechanismsupporting
confidence: 75%
“…Site-directed mutagenesis of residue Asp 33 in F-1,6-P aldolase results in a large drop in catalytic activity, and it had been proposed that this residue might act as proton acceptor from the C4 hydroxyl of the substrate during catalysis (Morris & Tolan, 1993). Mechanistic proposals for the catalytic role of Glu 187 in F-1,6-P aldolase include the maintenance of a neutral electrostatic potential at the active site (Littlechild & Watson, 1993) or participation in the dehydration step of the carbinolamine (Gefflaut et al, 1995).…”
Section: Proposed Mechanismmentioning
confidence: 99%
“…Surprisingly, in the same time, the preparation and evaluation of dozens of nonselective inhibitors of FBA have been reported. 10 We reasoned that an "ideal" selective inhibitor should have the following characteristics:…”
mentioning
confidence: 99%
“…1 Different from the members of the class II adolase family, transaldolase is characterized by the formation of a covalent Schiff base intermediate between a lysine residue within the active site and the substrate. [2][3][4] As a key enzyme in the pentose phosphate pathway, transaldolase catalyzes the reversible transfer of a dihydroxyacetone moiety from fructose 6-phosphate to erythrose 4-phosphate and forms sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate, respectively. 4-6 The vital functions of this enzyme are reported to balance the levels of NADPH and reactive oxygen intermediates (ROI) in the pentose phosphate pathway of glucose metabolism 7 and also to maintain the mitochondrial transmembrane potential and sperm fertility.…”
Section: Introductionmentioning
confidence: 99%