Kinetics of tyrosine

K. J. Willis and A. G. Szabo, The fluorescence decay kinetics of tyrosinate and tyrosine hydrogen bonded complexes, J. Phys. Chem. 95, 1585-1589 (1991). 

M. Nakanishi, M. Kobayashi, M. Tsuboi, C. Takasaki, and N. Tamiya, Electronic spectroscopy and deuteration kinetics of tyrosine and tryptophan residues An application to the study of erabutoxin b. Biochemistry 19, 3204-3208 (1980). 

X0vanadates, which may result in irreversible inhibition of some protein tyrosine phosphatases, as opposed to the readily reversible phosphatase inhibition seen with vanadates. In addition, vanadate s substitution for phosphate within the enzyme structure may result in formation of a transition state analog of protein tyrosine phosphatase, thus changing the kinetics of tyrosine kinase activation, and effectively acting as a means of fine tuning the intracellular balance between phosphatase inhibition and kinase activation. ... 

---

See also in sourсe #XX -- [ ]

---