Hydrolysis of phosphohistidine in water and in prostatic acid phosphatase.
Calculation of the free energy profile for hydrolysis of phosphohistidine using ONIOM methodology indicates a much tighter transition state in the enzyme active site compared to that in explicit water and elucidates the role of active site residues in catalysis.
Biocenter Oulu and the Department of Biochemistry, PL 3000, University of Oulu, FI-90014, Finland.
Satyan
S
Sharma
André H
AH
Juffer
D000135:Acid Phosphatase; D055162:Biocatalysis; D020134:Catalytic Domain; D006639:Histidine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D014867:Water / Q000737:chemistry*
D014867:Water; D006639:Histidine; D000135:Acid Phosphatase; C428439:prostatic acid phosphatase; D017027:Protein Tyrosine Phosphatases; C005436:phosphohistidine