Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Reaction

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 19 > >>
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate activation mechanism 652498
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate arrangement of two metal ions, a phosphate ion, and amino acid residues in the catalytic site is identical to that of PS/Tpases 665427
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate comparison of kinetic properties of different transmembrane and cytosolic isozymes 650430
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate conformation of active site is favorable for phosphotyrosine binding. Interaction of D115 and R13 to stabilize the conformation of the active cavity. A41 and G45 form a noncharged surface around the active cavity, which is surrounded by a flexible wall made of the loop region from F40 to T48 665402
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate for both alkyl and aryl substrates, including the activated substrate 4-nitrophenyl phosphate with its particularly good leaving group, general acid catalysis in PTPs is highly efficient and fully neutralizes the leaving group in the transition state. Mutating the conserved aspartic acid to glutamine causes the expected reductions in rate of several orders of magnitude and loss of the basic limb in pH-rate profiles, kinetic isotope effects, general acid catalysis mechanism, overview -, 749953
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate H148 acts as a general acid catalyst, D115 assists the protonation of the leaving group of a substrate, and D76 and D112 are involved in binding of magnesium ions 664363
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate in addition to active site, enzyme has a low-affinity noncatalytic aryl phosphate-binding site 664310
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism 650928, 652000, 94997, 95002
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism of the dephosphorylation catalysed by MptpA 714454
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.48[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism, features required for substrate 652017
Results 1 - 10 of 19 > >>