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Engineering of halophilic enzymes: Two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics toHalomonasandPseudomonasnucleoside diphosphate kinases
- Source :
- Protein Science. 17:1603-1610
- Publication Year :
- 2008
- Publisher :
- Wiley, 2008.
-
Abstract
- Nucleoside diphosphate kinase from Halomonas sp. 593 (HaNDK) exhibits halophilic characteristics. Residues 134 and 135 in the carboxy-terminal region of HaNDK are Glu–Glu, while those of its homologous counterpart of non-halophilic Pseudomonas NDK (PaNDK) are Ala–Ala. The double mutation, E134A-E135A, in HaNDK results in the loss of the halophilic characteristics, and, conversely, the double mutation of A134E-A135E in PaNDK confers halophilic characters to this enzyme, indicating that the charged state of these two residues that are located in the C-terminal region plays a critical role in determining halophilic characteristics. The importance of these two residues versus the net negative charges will be discussed in relation to the halophilicity of NDK.
- Subjects :
- Protein Denaturation
Hot Temperature
Time Factors
Amino Acids, Acidic
Molecular Sequence Data
Protein Renaturation
Sodium Chloride
Biology
Protein Engineering
medicine.disease_cause
Biochemistry
Protein Structure, Secondary
Article
Pseudomonas
Enzyme Stability
Escherichia coli
medicine
Amino Acid Sequence
Isoelectric Point
Molecular Biology
Peptide sequence
chemistry.chemical_classification
Halomonas
Dose-Response Relationship, Drug
Kinase
biology.organism_classification
Nucleoside-diphosphate kinase
Halophile
Molecular Weight
Enzyme
Solubility
chemistry
Nucleoside-Diphosphate Kinase
Mutation
Subjects
Details
- ISSN :
- 1469896X and 09618368
- Volume :
- 17
- Database :
- OpenAIRE
- Journal :
- Protein Science
- Accession number :
- edsair.doi.dedup.....dd03e641fa5486f9dc27f146e35fceec