2000
DOI: 10.1074/jbc.275.25.18939
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Free Energy Requirement for Domain Movement of an Enzyme

Abstract: The induced fit movement of an enzyme molecule upon the binding of substrate (1) has been characterized for many enzymes and is essential for catalysis. Domain closure of such enzymes can drastically change their active site environment from hydrophilic to hydrophobic, and such closure allows the enzymes to undergo reactions that are difficult in the aqueous phase. In order to elucidate the detailed mechanism of a given enzyme, it is necessary to estimate quantitatively the energy required for domain movement.… Show more

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Cited by 8 publications
(4 citation statements)
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References 37 publications
(63 reference statements)
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“…In all cases, interaction with the substrate aldimine might require closure of the active site channel to bring them into close proximity. This effect has been observed most notably in E. coli aspartate aminotransferase where the residue R292 undergoes large movements upon substrate binding leading to formation of the closed complex (Kirsch et al , 1984; Ishijima et al , 2000).…”
Section: Resultsmentioning
confidence: 95%
“…In all cases, interaction with the substrate aldimine might require closure of the active site channel to bring them into close proximity. This effect has been observed most notably in E. coli aspartate aminotransferase where the residue R292 undergoes large movements upon substrate binding leading to formation of the closed complex (Kirsch et al , 1984; Ishijima et al , 2000).…”
Section: Resultsmentioning
confidence: 95%
“…This observation indicates that only large ligands may cause this N-terminal α-helix shift. In E. coli aspartate aminotransferase, domain movement was changed dramatically from an open to a closed form by the addition of only one CH 2 to the side chain of the C4 substrate CH 3 (CH 2 )C α H(NH 3 ) + COO − 47. Taken together, these results indicate that one of the two substrates (α-ketoacid and amino acid) must be big enough to initiate the conformational change in order for the transamination reaction to happen.…”
Section: Discussionmentioning
confidence: 96%
“…Results and Discussion Aspartate aminotransferase from the mesophile Escherichia coli (EcAT) consists of two domains, which close upon substrate binding [1,2]. Recently, we were able to estimate the free energy required for domain movement by means of kinetic studies in a series of aliphatic substrates and corresponding crystallographic studies [3]. Upon binding of the acidic substrate, the side chain of Arg292* largely moves into the active site to create bifurcated hydrogen bonds and an electrostatic interaction with the distal carboxylate (ω-carboxylate) group of the bound acidic substrate.…”
Section: Methodsmentioning
confidence: 99%