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.
Sharma
Satyan
S
Biocenter Oulu and the Department of Biochemistry, PL 3000, University of Oulu, FI-90014, Finland.
Juffer
André H
AH
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