Specification of amino acid residues essential for the catalytic reaction of cold-active protein-tyrosine phosphatase of a psychrophile, Shewanella sp.
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.
Tsuruta
Hiroki
H
Center for Cooperative Research and Development, Kobe University, Japan. tsuruta@ans.kobe-u.ac.jp
Tamura
Jun
J
Yamagata
Hiroshi
H
Aizono
Yasuo
Y
D000596:Amino Acids / Q000737:chemistry*; D002384:Catalysis; D003080:Cold Temperature; D005982:Glutathione Transferase / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D020592:Shewanella / Q000201:enzymology*; D013696:Temperature
D000596:Amino Acids; D005982:Glutathione Transferase; D010744:Phosphoric Monoester Hydrolases; D017027:Protein Tyrosine Phosphatases