Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli

@article{Berry1993IdentificationOZ,
  title={Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli},
  author={Alan Berry and Karen E Marshall},
  journal={FEBS Letters},
  year={1993},
  volume={318}
}
An expression and mutagenesis system for the E. coli Class II fructose‐1,6‐bisphosphate aldolase has been created by modification of the vector pKfda (Biochem. J. 257 (1989) 529‐534). Large amounts of Class II aldolase (about 1 g/l in crude extracts), with properties consistent with those previously reported for the naturally occurring enzyme (Biochem. J. 169 (1978) 633‐641) are obtained. The enzyme contains 2 zinc ions per enzyme dimer. We have investigated the nature of the zinc‐binding site… Expand
Identification of arginine 331 as an important active site residue in the Class II fructose‐1,6‐bisphosphate aldolase of Escherichia coli
TLDR
Results show that Arg‐331 is critically involved in the binding of fructose bisphosphate by the enzyme and demonstrate that it interacts with the C‐6 phosphate group of the substrate. Expand
Conserved residues in the mechanism of the E. coli Class II FBP-aldolase.
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Fourier transform infra-red spectroscopy of the wild-type and mutant enzymes has further delineated the role of Asp109 as being critically involved in the polarisation of the carbonyl group of glyceraldehyde 3-phosphate. Expand
Fructose‐1,6‐bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli
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The primary site of nickel toxicity in E.’coli is defined as the class II aldolase FbaA through binding to the non‐catalytic zinc site. Expand
Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases.
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The X-ray structure has been used, together with sequence alignments, site-directed mutagenesis and steady-state enzyme kinetics to extend studies to map important residues in the binding of glyceraldehyde 3-phosphate, and shows that the two aldolases are highly discriminating between the diastereoisomers fructose bisph phosphate and tagatose bisphosphates. Expand
A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli.
TLDR
The measurement of deuterium kinetic isotope effects using [1(S)-(2)H]DHAP showed that, for the wild-type enzyme, proton abstraction was not the rate determining step, whereas in the case of the E182A mutant this step had become rate limiting, providing evidence for the role of Glu182 in abstraction of the C1 proton from DHAP in the condensation direction of the reaction. Expand
The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.
TLDR
Comparison of the structure with a class II fuculose aldolase suggests that these enzymes may share a common mechanism, and the class II enzymes should be subdivided into two categories on consideration of subunit size and fold, quaternary structure and metal-ion binding sites. Expand
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TLDR
The fructose-1,6-bisphosphate aldolase gene from the thermophilic bacterium, Anoxybacillus gonensis G2, was cloned and sequenced and the activity of enzyme was completely inhibited by EDTA. Expand
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TLDR
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TLDR
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