Protein tyrosine phosphatases: mechanisms of catalysis and regulation
JM Denu, JE Dixon - Current opinion in chemical biology, 1998 - Elsevier
JM Denu, JE Dixon
Current opinion in chemical biology, 1998•ElsevierRecent structural information suggests that the HC (X) 5R active-site motif defines three
distinct evolutionary families of phosphatases that employ a common catalytic mechanism.
In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms
involving either intermolecular or intramolecular interactions, whereby inhibition is mediated
by sterically blocking the active-site cleft.
distinct evolutionary families of phosphatases that employ a common catalytic mechanism.
In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms
involving either intermolecular or intramolecular interactions, whereby inhibition is mediated
by sterically blocking the active-site cleft.
Recent structural information suggests that the HC(X)5R active-site motif defines three distinct evolutionary families of phosphatases that employ a common catalytic mechanism. In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms involving either intermolecular or intramolecular interactions, whereby inhibition is mediated by sterically blocking the active-site cleft.
Elsevier