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The Effect of Hydrophobic Interactions in the Subunit Interphase of Thermoplasma acidophilum Citrate Synthase on Thermostability
Date
1997-08-17
Author
Kocabıyık, Semra
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https://hdl.handle.net/11511/70591
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The effect of cysteine-43 mutation on thermostability and kinetic properties of citrate synthase from Thermoplasma acidophilum
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In this study, we have substituted serine-43 by cysteine in the recombinant citrate synthase from a moderately thermophilic Archaeon Thermoplasma acidophilum, for site-specific attachment of labels and have investigated the effects of this mutation on the biochemical properties and thermal stability of the enzyme. Both wild-type and the mutant enzymes were purified to homogenity using affinity chromatography on Matrex Gel Red A. The mutant Thermoplasma citrate synthase is very similar to wild-type citrate s...
The effect of hydrophobic interactions in the dimer interface of Thermoplasma acidophilum citrate synthase on thermostability.
Erduran, I; Kocabıyık, Semra (1998-08-01)
The effect of valine substitution for glycine in the dimer interface of citrate synthase from Thermoplasma acidophilum on stability and activity
Kocabıyık, Semra (Elsevier BV, 2000-08-28)
To determine the role of hydrophobic interactions in the dimer interface of citrate synthase (CS) from Thermoplasma (Tp) acidophilum in thermostabilization, we have used site-directed mutagenesis to replace Gly 196 by Val on the helix L of the subunit interface. Recombinant wild-type and Gly 196 mutant TpCS enzymes were largely identical in terms of substrate specificities (K-m for oxaloacetate and acetyl CoA). However, the mutation not only reduced catalytic activity (about 10-fold) (i.e., V-max, K-cat and...
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S. Kocabıyık, “The Effect of Hydrophobic Interactions in the Subunit Interphase of Thermoplasma acidophilum Citrate Synthase on Thermostability,” 1997, Accessed: 00, 2021. [Online]. Available: https://hdl.handle.net/11511/70591.