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Results 1 - 10 of 17 > >>
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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6A513T mutant associated with congenital myasthenic syndrome, shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition 756802
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6H268L an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 487318
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6H268N an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 487318
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6H393L an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 487318
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6H393N an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 487318
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6H426L an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 487318
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6H426N an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426 487318
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6N514R is described as ChAT-R, the introduction of an Arg at position 514 in rat enzyme is predicted to provide the ionic charge required to interact with, and neutralize, the carboxyl group of carnitine 487328
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6P17A/P19A mutant shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition 756802
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.6R452A kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues 487331
Results 1 - 10 of 17 > >>
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