Specification of Amino Acid Residues Essential for the Catalytic Reaction of Cold-active Protein-tyrosine Phosphatase of a Psychrophile,Shewanellasp
| Autor: | Hiroki Tsuruta, Yasuo Aizono, Hiroshi Yamagata, Jun Tamura |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Shewanella
Phosphatase Protonation Protein tyrosine phosphatase Biology Applied Microbiology and Biotechnology Biochemistry Catalysis Analytical Chemistry Amino Acids Psychrophile Site-directed mutagenesis Molecular Biology Magnesium ion Peptide sequence Glutathione Transferase Reverse Transcriptase Polymerase Chain Reaction Organic Chemistry Temperature General Medicine biology.organism_classification Phosphoric Monoester Hydrolases Cold Temperature Mutagenesis Site-Directed Protein Tyrosine Phosphatases Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 68:440-443 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.68.440 |
| Popis: | Protein-tyrosine phosphatase [EC 3.1.3.48] from a psychrophile, Shewanella sp. shows high activity at low temperatures and has the conserved amino acid sequence of protein-Ser/Thr-phosphatases. Site-directed mutagenesis with the conserved amino acid residues indicated that His148 could be important as a general acid catalyst and Asp115 assists the protonation with His148 of the leaving group of a substrate, and that Asp76 and Asp112 were involved in binding to magnesium ions. |
| Databáze: | OpenAIRE |
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