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Results 1 - 8 of 8
EC Number
Reaction
Commentary
Reference
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
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ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
catalytic mechanism
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
reaction mechanism
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
regulation of enzyme activity involves the activation loop, a polypeptide region outside the active site cleft, which is reversibly phosphorylated
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
residue W1038 is essential for catalytic activity
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
structure-function relation ship, active site structure, catalytic mechanism involving the catalytic base Asp386 and enzyme regulation, overview
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
structure-function relationship, active site structure, catalytic mechanism and enzyme regulation, overview
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
substrate binding site involving residues R279, R281, and R283, more distant residues S280, F382, S273, and D276 are also important for activity
Results 1 - 8 of 8