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

BRENDA support

Refine search

Search Protein Variants

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 35 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103C38D site-directed mutagenesis 285702
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103C38S 1 cysteine residue per subunit is essential for catalytic activity and Mn2+ binding 285704
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103C38S site-directed mutagenesis, catalytically inactive mutant, C38 is located in an activating divalent metal-ion binding site 285702
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103D179A mutation affects switching between the open and closed form of the enzyme. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 36fold lower than wild-type value 762728
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103D179N mutation affects switching between the open and closed form of the enzyme. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 190fold lower than wild-type value 762728
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103D180A 228fold decrease in the catalytic efficiency -, 762551
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103E152A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme 687461
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103E152C site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme 687461
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103E152D site-directed mutagenesis, the E152D mutant shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD+ compared to wild-type TDH, Glu152 to Asp substitution causes the enhancement of deprotonation of His47 or ionization of zinc-bound water and threonine in the enzyme-NAD+ complex 687461
Show all pathways known for 1.1.1.103Display the reaction diagram Show all sequences 1.1.1.103E152K site-directed mutagenesis, inactive mutant 687461
Results 1 - 10 of 35 > >>