Amino Acid Substitutions in the Subunit Interface Enhancing Thermostability of Thermoplasma acidophilum Citrate Synthase

1998-07-05

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Amino acid substitutions in the subunit interface enhancing thermostability of Thermoplasma acidophilum citrate synthase
Erduran, I; Kocabıyık, Semra (Elsevier BV, 1998-08-19)
We have used citrate synthase from Thermoplasma (Tp.) acidophilum as a thermostable model system to investigate the role of hydrophobic interactions in dimer interface for maintaining high temperature stability. Three mutant enzymes were constructed by single amino acid substitutions in the interface helices: Ala97 --> Ser, Ala104 --> Thr, and Gly209 --> Ala. All of the mutations enhanced the thermostability of Tp. citrate synthase, while improving its catalytic properties (K-m, V-max, and specific activity...
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AMINO-ACID SUBSTITUTIONS WITHIN THE ANALOGOUS NUCLEOTIDE-BINDING LOOP (P-LOOP) OF AMINOGLYCOSIDE 3'-PHOSPHOTRANSFERASE-II
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1. Oligonucleotide-directed mutagenesis of APH(3')-II was used to investigate the functions of key amino acids in the P-loop analogous motif of the enzyme. 2. The mutations of Gly205 --> GIu, Gly210 --> Ala and Arg211 --> Pro considerably reduced the resistance of the resulting strains to KM and to related drugs, e.g. G418. 3. Similarly, enzyme activity in the crude extracts of these mutants was substantially reduced as well as the enzyme's affinity for Mg2+ ATP. 4. Alternatively substitutions at a highly c...
Citation Formats
S. Kocabıyık, “Amino Acid Substitutions in the Subunit Interface Enhancing Thermostability of Thermoplasma acidophilum Citrate Synthase,” 1998, Accessed: 00, 2021. [Online]. Available: https://hdl.handle.net/11511/77806.