The Effect of Cysteine 43 Mutation on Catalytic Properties and Thermostability of Thermoplasma acidophilum Citrate Synthase

Date

1996-07-07

Author

Kocabıyık, Semra

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https://hdl.handle.net/11511/72389

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The effect of cysteine 43 mutation on catalytic properties and thermostability of thermoplasma acidophilum citrate synthase Erduran, ipek; Kocabıyık, Semra; Department of Biology (1996)
The effect of arginine-428 mutation on modulation of activity of human liver flavin monooxygenase 3 (FMO3) by imipramine and chlorpromazine Adalı, Orhan; Philpot, RM (1999-07-01) This study was carried out to investigate the molecular basis for modulation of recombinant FMO3-catalyzed activity by the tricyclicantidepressants, imipramine and chlorpromazine. A mutant of human liver FMO3 (T428R) was formed by site-directed mutagenesis and characterized along with the native enzyme in order to elucidate a possible structure-function relationship. Functional properties of native and T428R human FMO3s were studied with methimazole as substrate. Both enzymes catalyzed the S-oxidation of me...
The effect of cysteine-43 mutation on thermostability and kinetic properties of citrate synthase from Thermoplasma acidophilum Kocabıyık, Semra; Russel, RJM; Danson, MJ; Hough, DW (Elsevier BV, 1996-07-05) 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 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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Citation Formats

S. Kocabıyık, “The Effect of Cysteine 43 Mutation on Catalytic Properties and Thermostability of Thermoplasma acidophilum Citrate Synthase,” 1996, Accessed: 00, 2021. [Online]. Available: https://hdl.handle.net/11511/72389.